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Photochemical Ribonucleotide Reductase For The Study Of Proton Coupled Electron Transfer
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Book Synopsis Photochemical Ribonucleotide Reductase for the Study of Proton-coupled Electron Transfer by : Steven Y. Reece
Download or read book Photochemical Ribonucleotide Reductase for the Study of Proton-coupled Electron Transfer written by Steven Y. Reece and published by . This book was released on 2007 with total page 232 pages. Available in PDF, EPUB and Kindle. Book excerpt: (Cont.) To study the mechanism of this radical transport, we have developed photochemical RNRs wherein radical generation, transport, and enzymatic turnover can be initiated by UV-vis excitation of a peptide bound to the subunit containing the enzyme active site. This method allows us to observe Y*s competent for initiating turnover on the peptide bound to the protein subunit. Turnover assays with the wild-type and mutant proteins show that both the electron and proton move along a unidirectional pathway to affect radical transport in this subunit.
Book Synopsis Photoinitiated Proton-coupled Electron Transfer and Radical Transport Kinetics in Class la Ribonucleotide Reductase by : Arturo Alejandro Pizano
Download or read book Photoinitiated Proton-coupled Electron Transfer and Radical Transport Kinetics in Class la Ribonucleotide Reductase written by Arturo Alejandro Pizano and published by . This book was released on 2013 with total page 202 pages. Available in PDF, EPUB and Kindle. Book excerpt: Proton-coupled electron transfer (PCET) is a critical mechanism in biology, underpinning key processes such as radical transport, energy transduction, and enzymatic substrate activation. Ribonucleotide reductases (RNRs) rely on PCET to mediate the rate-limiting step in the synthesis of DNA precursors. E. coli class Ia RNR consists of two dimeric subunits: [alpha]2 contains the active site, while [beta]2 contains a stable diferric-tyrosyl radical cofactor. During turnover, transport occurs over 35 Ȧ, from Y122 in [beta]2 to C439 in [alpha]2) where an active-site thiyl radical mediates turnover. Radical transport is proposed to occur over a series of highly conserved redox-active amino acids, including Y356 in [beta]2,and Y731 and Y730 in [alpha]2 . This thesis examines three subject areas of PCET that pertain to RNR: Small-molecule model systems provide insights into tyrosine oxidation and radical generation. Under physiological conditions, tyrosine oxidation is accompanied by deprotonation and occurs by PCET. A critical factor in PCET reactions is the nature ofthe proton acceptor and the presence ofhydrogen bonding. In a modular model system, pyridyl-amino acid-methyl esters are appended to rhenium(I) tricarbonyl phenanthroline to yield rhenium-amino acid complexes. In dichloromethane solution, bases coordinate to tyrosine by hydrogen bonding. Emission kinetics reveal base-dependent oxidation by PCET. A photopeptide composed of the 19 C-terminal residues of [beta]2, fluorinated tyrosine in place of Y356, and a rhenium(I) bipyridine photooxidant enables photoinitated radical transport into [alpha]2. Transient absorption kinetics show rapid radical transport (105 s-1) that is only observed when both Y731 and Y730, are present, suggesting a critical role for the Y731-Y730, dyad for radical transport in RNR. An intact, photochemical [beta]2 enables studies of an [alpha]2:[beta]2 complex. A bromomethylpyridine rhenium(I) phenanthroline photooxidant labels a single surface-cysteine mutant of [beta]2 at position 355 to yield [Re]- [beta]2. Under flash-quench conditions, transient absorption reveals a tyrosine radical. [Re] -[beta]2 binds [alpha]2 and is capable of light-initiated substrate turnover. Transient emission quenching experiments reveal Y356 oxidation that is dependent on the presence of Y731 in [alpha]2. This result suggests that a Y356-Y731-Y730 triad mediates radical transport across the subunit interface and into [alpha]2.
Book Synopsis Mechanistic Studies of Proton-coupled Electron Transfer in Aminotyrosine- and Fluorotyrosine- Substituted Class Ia Ribonucleotide Reductase by : Ellen Catherine Minnihan
Download or read book Mechanistic Studies of Proton-coupled Electron Transfer in Aminotyrosine- and Fluorotyrosine- Substituted Class Ia Ribonucleotide Reductase written by Ellen Catherine Minnihan and published by . This book was released on 2012 with total page 398 pages. Available in PDF, EPUB and Kindle. Book excerpt: Ribonucleotide reductase (RNR) catalyzes the conversion of nucleotides to 2'- deoxynucleotides in all organisms. The class Ia RNR from Escherichia coli is active as an a2p2 complex and utilizes an unprecedented mechanism of reversible proton-coupled electron transfer (PCET) to propagate a stable tyrosyl radical (Yi22-) in P2 over a distance of >35 A to an active site cysteine (C4 3 9) in a2 on each turnover. Generation of the cysteinyl radical (C4 3 9-) initiates active site nucleotide reduction. Radical propagation over 35 A by a pure tunneling mechanism would be too slow to support the observed turnover number. Instead, long-range, reversible PCET is proposed to occur by radical hopping along a specific pathway of redox-active amino acids: ... The details of this mechanism are kinetically masked in wild-type RNR, and mutation of any of these residues to another native amino acid inactivates the enzyme. Recent development of technology for the in vivo, site-specific incorporation of unnatural amino acids into proteins has provided the opportunity to systematically perturb the native PCET pathway by introduction of tyrosine analogues with modified redox potentials and/or pKas. This thesis focuses on 3-aminotyrosine (NH2Y) and fluorotyrosines (FnYs). NH2Y has a lower reduction potential than Y and, when incorporated at the three sites of transient Ye formation, generates a thermodynamic minimum and reduces kcat sufficiently to allow characterization of NH2Y. intermediates. A kinetic model for catalysis by NH2Y-RNRs has been proposed from the mechanistic studies described herein. Furthermore, the ability to generate NH2Y* on the pathway has afforded the first characterization of a kinetically stable c2p2 complex. FnYs span a wide range of solution pKas and reduction potentials and thus may be used to investigate both PT and ET events. The evolution of an orthogonal, polyspecific tRNA/tRNA synthetase pair for FnYs is reported. FnYs at positions 356, 730, and 731 have been used to measure the pH dependence of RNR activity, whereas FnY-s at position 122 of $2 have been used as radical initiators to begin mapping the relative thermodynamic landscape of the PCET pathway.
Book Synopsis Kinetics and Dynamics Controlling Proton-coupled Electron Transfer in Ribonucleotide Reductase by : Lisa Olshansky
Download or read book Kinetics and Dynamics Controlling Proton-coupled Electron Transfer in Ribonucleotide Reductase written by Lisa Olshansky and published by . This book was released on 2015 with total page 310 pages. Available in PDF, EPUB and Kindle. Book excerpt: Proton-coupled electron transfer (PCET) reactions comprise a fundamental mechanism for energy transduction in nature. In catalyzing the conversion of ribonucleotides to deoxyribonucleotides, ribonucleotide reductase (RNR) performs reversible, long-range PCET over a pathway of redox active amino acids ([beta]-Y122 >/ [beta]-Y356 / [alpha]-Y731 / [alpha]-Y730 /
Book Synopsis The Development and Analysis of Model Systems to Probe Proton-Coupled Electron Transfer in Ribonucleotide Reductase Ia of E. Coli by : Bon Jun Koo
Download or read book The Development and Analysis of Model Systems to Probe Proton-Coupled Electron Transfer in Ribonucleotide Reductase Ia of E. Coli written by Bon Jun Koo and published by . This book was released on 2016 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: Proton-coupled electron transfer (PCET) combines proton transfer with electron transfer to bypass high-energy intermediates. The ribonucleotide reductase (RNR) family of enzymes catalyzes the conversion of ribonucleotides to deoxynucleotides using amino acid radicals. The enzyme contains an efficient PCET pathway that transfers an electron and proton over a 35 Å distance across two subunits, the longest PCET pathway known in biology. The enzyme func-tions with very high fidelity, performing >105 turnovers before radical loss.
Book Synopsis Proton-coupled Electron Transfer in the Escherichia Coli Ribonucleotide Reductase by : Michelle Chia-yu Chang
Download or read book Proton-coupled Electron Transfer in the Escherichia Coli Ribonucleotide Reductase written by Michelle Chia-yu Chang and published by . This book was released on 2004 with total page 578 pages. Available in PDF, EPUB and Kindle. Book excerpt: (Cont.) Mutation of conserved tyrosines on the pathway, corresponding to Y356 and Y731, to phenylalanine effectively deactivates radical initiation. These results provide the first direct evidence of the radical transfer pathway of the class I RNRs and underscore the importance of aromatic amino acid radical intermediates for proton-coupled electron transfer in physiologically-relevant processes.
Book Synopsis Mechanistic Investigations of the Radical Transport Pathway in Fluorotyrosine-substituted Class Ia Ribonucleotide Reductases by : Kanchana Ravichandran
Download or read book Mechanistic Investigations of the Radical Transport Pathway in Fluorotyrosine-substituted Class Ia Ribonucleotide Reductases written by Kanchana Ravichandran and published by . This book was released on 2016 with total page 326 pages. Available in PDF, EPUB and Kindle. Book excerpt: Ribonucleotide reductase (RNR) catalyzes the reduction of nucleotides to 2'- deoxynucleotides, providing the monomeric precursors for DNA replication and repair. The focus of this thesis is on the E. coli class la RNR that is composed of two homodimeric subunits ([alpha]a2 and [beta]2), which form an active [alpha]2[beta]2 complex. A stable diferric-tyrosyl radical (Y122*) in [beta]2 reversibly oxidizes an active site cysteine (C439*) in [alpha]2 via multiple proton-coupled electron transfer (PCET) steps through conserved aromatic amino acid residues: Y122* - [W48] - Y356 in [beta]2 to Y731 - Y730 - C439 in [alpha]2. The transient C439* is responsible for initiating nucleotide reduction. Long-range radical transport (RT) and nucleotide reduction are kinetically masked by rate-limiting protein conformational changes. Herein, the stable Y1228 is site-specifically replaced with a 2,3,5-trifluorotyrosyl radical (2,3,5-F3Y*) that modulates the driving force for RT. This 2,3,5-F3Y-substituted RNR perturbs PCET kinetics such that a radical intermediate (Y356*) can be observed and characterized. Rapid kinetic studies demonstrate that Y356* is kinetically and chemically competent for nucleotide reduction, and provide the first evidence for a pathway Yo that can complete the RNR catalytic cycle. Temperature and pH dependent studies show equilibration of the stable 2,3,5-F3Y* with the pathway radical intermediate, Y356*. These data are corroborated by similar experiments performed with 3,5-difluorotyrosine (3,5-F2Y) in place of Y356, which demonstrate equilibration of Y122*. with 3,5-F2Y*. These studies together provide insight into the thermodynamic landscape of the RT pathway. A model is proposed in which the RT pathway is thermodynamically uphill and driven forward by rapid irreversible water loss that occurs during nucleotide reduction. The 3,5-F2Y analog is further utilized to test the ability of E350, a conserved [beta]2 C-terminal tail residue, to function as the proton acceptor for Y356 or Y731 . A model is put forth in which E350 does not participate in proton transfer, but is involved in [alpha]2[beta]2 subunit interaction and in controlling radical initiation. Finally, an X-ray crystal structure of the active [alpha]2[beta]2 complex has remained elusive. Herein, Ni-NTA pull-down assays are presented, demonstrating that injection of a single electron into the diferric cluster site generates a stable [alpha]2[beta]2 complex. These studies afford the opportunity to structurally characterize the [alpha]2[beta]2 complex with the goal of understanding PCET across the [beta]a interface.
Book Synopsis Mechanistic Studies of the Class I Ribonucleotide Reductases from S. Cerevisiae and E. Coli by : Jie Ge
Download or read book Mechanistic Studies of the Class I Ribonucleotide Reductases from S. Cerevisiae and E. Coli written by Jie Ge and published by . This book was released on 2003 with total page 423 pages. Available in PDF, EPUB and Kindle. Book excerpt: (Cont.) The results of initial studies on the energetics of heterodimer formation using calorimetric techniques and site-directed mutagenesis are discussed in the context of the structures of Y2Y2, Y2Y4, and Y4Y4. As the discovery of a second R2 subunit is not unique to S. cerevisiae, the potential implication of the heterodimer in the regulation of deoxyribonucleotide synthesis is also considered. In the second part of this thesis, pre-steady state kinetics of the class I E. coli RNR is investigated using stopped-flow UV-visible spectroscopy and rapid chemical quench methods. These studies have led to a model in which the rate determining step in catalysis is a physical step prior to proton-coupled electron transfer (PCET), nucleotide reduction, and reverse PCET. These results provide a crucial first step in understanding radical initiation over 35 [angstroms].
Book Synopsis Class Ic Ribonucleotide Reductases by : Jovan Livada
Download or read book Class Ic Ribonucleotide Reductases written by Jovan Livada and published by . This book was released on 2019 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: Ribonucleotide reductases (RNRs) are the only known catalysts that are capable of the life essential conversion of ribonucleotides to deoxyribonucleotides. All RNRs use a transient cysteine radical (C) to initiate the catalytic cycle. Based on the method of generation of the C, RNRs are divided into three (I, II, III) major classes. Class III RNRs use an Fe4S4 cluster in tandem with an S-adenosyl-L-methionine radical activase to install a glycyl radical that is stable in anoxic conditions. In class III RNRs this glycyl radical is the active oxidant that forms the C. The active oxidant in class II RNRs is 5-deoxyadenosylcob(III)alamin which generates the C via the reversable Co-C bond homolytic cleavage. Class I RNRs are the sole focus of this study and they contain two subunits, a smaller subunit that contains the active oxidant and usually hosts a dimetal center, and the larger subunit that harbors the substrate binding site and contains the key cysteine residue that is transiently oxidized during catalysis.All class I RNRs use the active oxidant in their smaller subunit to transiently oxidize the C in the larger subunit that is ~35 away. This is a multi-step, long range electron transfer process coupled by a few local proton transfers and mediated by, at a minimum, one tyrosine residue in and two tyrosine residues in . Class I RNRs are further subdivided into five subclasses (a-e) that differ in four relevant properties. One, the nature of the active oxidant in (Y, MnIV or DOPA), two, the presence of a dimetal cofactor (Fe/Fe, Mn/Mn, Mn/Fe, or none), three, the oxygen species required for the formation of the active oxidant (O2 or O2-), and four, the requirement of an activase protein, NrdI. Archetypical class Ia RNRs generate the active oxidant, Y, via the use of a -FeII/FeII cofactor and O2. On the other hand, class Ic RNRs, the main topic of this study, use a heterobinuclear -MnII/FeII cofactor that is activated in the reaction with dioxygen and via the -MnIV/FeIV intermediate form the active cofactor -MnIV/FeIII, where MnIV represents the active oxidant.RNR subclasses Ia, Ib, Id and Ie all have a minimum of three members verified by in vitro characterization, while the RNR from Chlamydia trachomatis (Ct) remains the sole verified example of class Ic ribonucleotide reductases, discovered in 2007. In this work, twelve years later, we have introduced a second class Ic RNR that uses a -MnIV/FeIII active cofactor from Gimesia maris (Gm), a heterotroph found in various aquatic locations around the US. Rapid kinetic methods, stopped-flow and freeze quench, Mssbauer, and electron paramagnetic resonance (EPR) spectroscopies as well as activity assay analysis were all used to characterize Gm RNR as a bona fide class Ic RNR. Like Ct, Gm RNR was shown to possess a branched electron relay pathway in that consist of two tyrosine residues and one tryptophan. Interestingly, by removing a subclass specific tyrosine residue involved in the cofactor reaction with dioxygen we were able to noticeably increase the rate of catalytic activity. This information sheds light onto the activating and catalytic electron relays in class Ic RNRs.Sequence similarity network analysis of genes that encode both for RNR and subunits indicate clusters of closely coevolved RNRs that belong to both class Ia and class Ic RNR subclasses. In vitro characterization of a tentative class Ia RNR from Methylococcus capsulatus (Mc) confirms that this RNR uses a Fe/Fe cluster to generate the nearby active Y oxidant. A closely co evolved RNR whose gene sequence suggests that it belongs to the class Ic RNR subclass from Salinisphaera hydrothermalis (Sh) was also characterized and confirmed that it forms a MnIV/FeIII cofactor and that it uses MnIV as the active oxidant. Activity assays have shown that both heterologous pairs of and subunits of Mc and Sh RNR are able to perform bidirectional radical translocation. This represents initial evidence that the multi-step, one electron, multiple proton transfer mechanism between and RNR subunits is conserved between the RNR subclasses Ia and Ic. We hypothesize that this mechanism might be conserved in all class I RNRs. Additionally, we concluded that there were no adaptations required, for performing ribonucleotide reduction, made to either subunit to accommodate a complementary subunit from a different subclass except for the evolution of the subunit to harbor a distinct active oxidant.The aforementioned multi-step, one electron, multiple proton transfer process is believed to involve a 35 distance between the active oxidant in and the catalysis initiating cysteine residue in . The active cofactor from the class Ic RNR from Chlamydia trachomatis -MnIV/FeIII is reduced to an EPR accessible (S = 1/2) MnIII/FeIII state in the subunit and generates a cysteinyl radical in the active site. The radical in the larger subunit can be trapped via a known mechanism based inactivator, 2-azido-2-deoxyuridine-5-diphosphate (N3UDP). The resulting reaction accumulates a stable, nitrogen-centered radical (N) in the active site of . Using double electronelectron resonance experiments, we have elucidated the distance between the -MnIII/FeIII cofactor in and N in to be 43 1 . This experimental investigation not only provides the first structural information concerning the class Ic RNR holoenzyme complex but also the first direct experimental measurement of the inter-subunit RT distance in any class I RNR.In class Ia RNRs, the first step of the bidirectional, multi-step, one electron, multiple proton transfer process has been characterized as a proton-coupled-electron-transfer (PCET) reaction where the active oxidant (Y) is reduced by a nearby organic residue in and a local proton transfer occurs from the water ligand bound to the -FeIII/FeIII cofactor onto the radical harboring tyrosine. The presumptive proton transfer step in class Ic, Ct RNR, in which reduction of a -MnIV/FeIII oxidant to an EPR-active (S = 1/2) -MnIII/FeIII state drives Cys oxidation in , is not understood. We have used advanced electron paramagnetic resonance spectroscopies as well as density-functional theory (DFT) calculations to analyze the -MnIII/FeIII RT product to determine the number and location of its protons. The correlation of our findings in addition to the previous structural characterization of the -MnIV/FeIII RT-reactant state led us to identify that the acceptor for the initial proton transfer step in class Ic RNRs is a hydroxide ligand on the MnIV.
Book Synopsis Biological Inorganic Chemistry by : Ivano Bertini
Download or read book Biological Inorganic Chemistry written by Ivano Bertini and published by University Science Books. This book was released on 2007 with total page 794 pages. Available in PDF, EPUB and Kindle. Book excerpt: Part A.: Overviews of biological inorganic chemistry : 1. Bioinorganic chemistry and the biogeochemical cycles -- 2. Metal ions and proteins: binding, stability, and folding -- 3. Special cofactors and metal clusters -- 4. Transport and storage of metal ions in biology -- 5. Biominerals and biomineralization -- 6. Metals in medicine. -- Part B.: Metal ion containing biological systems : 1. Metal ion transport and storage -- 2. Hydrolytic chemistry -- 3. Electron transfer, respiration, and photosynthesis -- 4. Oxygen metabolism -- 5. Hydrogen, carbon, and sulfur metabolism -- 6. Metalloenzymes with radical intermediates -- 7. Metal ion receptors and signaling. -- Cell biology, biochemistry, and evolution: Tutorial I. -- Fundamentals of coordination chemistry: Tutorial II.
Book Synopsis Theory and Applications of the Empirical Valence Bond Approach by : Fernanda Duarte
Download or read book Theory and Applications of the Empirical Valence Bond Approach written by Fernanda Duarte and published by John Wiley & Sons. This book was released on 2017-04-17 with total page 139 pages. Available in PDF, EPUB and Kindle. Book excerpt: A comprehensive overview of current empirical valence bond (EVB) theory and applications, one of the most powerful tools for studying chemical processes in the condensed phase and in enzymes. Discusses the application of EVB models to a broad range of molecular systems of chemical and biological interest, including reaction dynamics, design of artificial catalysts, and the study of complex biological problems Edited by a rising star in the field of computational enzymology Foreword by Nobel laureate Arieh Warshel, who first developed the EVB approach
Book Synopsis Biomedical Index to PHS-supported Research by :
Download or read book Biomedical Index to PHS-supported Research written by and published by . This book was released on 1993 with total page 1400 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Sulfhydryl Compounds—Advances in Research and Application: 2012 Edition by :
Download or read book Sulfhydryl Compounds—Advances in Research and Application: 2012 Edition written by and published by ScholarlyEditions. This book was released on 2012-12-26 with total page 717 pages. Available in PDF, EPUB and Kindle. Book excerpt: Sulfhydryl Compounds—Advances in Research and Application: 2012 Edition is a ScholarlyEditions™ eBook that delivers timely, authoritative, and comprehensive information about Sulfhydryl Compounds. The editors have built Sulfhydryl Compounds—Advances in Research and Application: 2012 Edition on the vast information databases of ScholarlyNews.™ You can expect the information about Sulfhydryl Compounds in this eBook to be deeper than what you can access anywhere else, as well as consistently reliable, authoritative, informed, and relevant. The content of Sulfhydryl Compounds—Advances in Research and Application: 2012 Edition has been produced by the world’s leading scientists, engineers, analysts, research institutions, and companies. All of the content is from peer-reviewed sources, and all of it is written, assembled, and edited by the editors at ScholarlyEditions™ and available exclusively from us. You now have a source you can cite with authority, confidence, and credibility. More information is available at http://www.ScholarlyEditions.com/.
Book Synopsis Expressed Protein Ligation by : Miquel Vila-Perelló
Download or read book Expressed Protein Ligation written by Miquel Vila-Perelló and published by Humana. This book was released on 2020-03-07 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book provides a comprehensive overview of Expressed Protein Ligation (EPL), detailing methods and protocols to generate site-specifically modified proteins. Chapters include an overview of the protein semi-synthesis field, as well as related areas that have contributed to the development of EPL such as protein splicing and peptide synthesis. Following the introductory chapters, the rest of the book guides readers through protocols to perform EPL reactions, methods to synthesize peptide thioesters and to perform peptide and protein ligations, label proteins inside living cells, protocols for the semi-synthesis of phorphorylated, glycosylated and ubiquitylated proteins, synthesis and assembly of assymetrically modified nucleosomes, use of ligation auxiliaries and synthesis of cyclic proteins, as well as novel desulfurization strategies and use of selective Cys side chain protection to obtain precisely modified proteins.Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and cutting-edge, Expressed Protein Ligation: Methods and Protocols will ensure successful implementation of protein semi-synthesis methods to further study the structure and function of proteins.
Book Synopsis With the R. N. R. by : " "Windlass (pseud.)
Download or read book With the R. N. R. written by " "Windlass (pseud.) and published by . This book was released on 1917 with total page 262 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Color Atlas of Biochemistry by : Jan Koolman
Download or read book Color Atlas of Biochemistry written by Jan Koolman and published by Thieme. This book was released on 2011-01-01 with total page 482 pages. Available in PDF, EPUB and Kindle. Book excerpt: Totally revised and expanded, the Color Atlas of Biochemistry presents the fundamentals of human and mammalian biochemistry on 215 stunning color plates.Alongside a short introduction to chemistry and the classical topics of biochemistry, the 2nd edition covers new approaches and aspects in biochemistry, such as links between chemical structure and biological function or pathways for information transfer, as well as recent developments and discoveries, such as the structures of many new important molecules. Key features of this title include:- The unique combination of highly effective color graphics and comprehensive figure legends;- Unified color-coding of atoms, coenzymes, chemical classes, and cell organelles that allows quick recognition of all involved systems;- Computer graphics provide simulated 3D representation of many important molecules.This Flexibook is ideal for students of medicine and biochemistry and a valuable source of reference for practitioners.
Book Synopsis Novel Cofactors by : Judith P. Klinman
Download or read book Novel Cofactors written by Judith P. Klinman and published by Gulf Professional Publishing. This book was released on 2001-10-05 with total page 502 pages. Available in PDF, EPUB and Kindle. Book excerpt: A cofactor is a component part of many enzymes and functions by uniting with another molecule in order to become active. The use of cofactors to supplement the native amino acids of a protein is essential to maintain the chemical capabilities necessary for organisms to survive. This volume focuses on the significant advances of the past decade in identifying and describing new cofactors--either small molecules or those derived posttranslationally.
