Search Results - "Davidson, Victor L"

Protein Control of True, Gated, and Coupled Electron Transfer Reactions by Davidson, Victor L

“…Electron transfer (ET) through and between proteins is a fundamental biological process. The rates of ET depend upon the thermodynamic driving force, the…”
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Diversity of structures, catalytic mechanisms and processes of cofactor biosynthesis of tryptophylquinone-bearing enzymes by Yukl, Erik T., Davidson, Victor L.

“…Tryptophyquinone-bearing enzymes contain protein-derived cofactors formed by posttranslational modifications of Trp residues. Tryptophan tryptophylquinone…”
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Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG by Geng, Jiafeng, Dornevil, Kednerlin, Davidson, Victor L., Liu, Aimin

“…The diheme enzyme MauG catalyzes posttranslational modifications of a methylamine dehydrogenase precursor protein to generate a tryptophan tryptophylquinone…”
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Acoustic Injectors for Drop-On-Demand Serial Femtosecond Crystallography by Roessler, Christian G., Agarwal, Rakhi, Allaire, Marc, Alonso-Mori, Roberto, Andi, Babak, Bachega, José F.R., Bommer, Martin, Brewster, Aaron S., Browne, Michael C., Chatterjee, Ruchira, Cho, Eunsun, Cohen, Aina E., Cowan, Matthew, Datwani, Sammy, Davidson, Victor L., Defever, Jim, Eaton, Brent, Ellson, Richard, Feng, Yiping, Ghislain, Lucien P., Glownia, James M., Han, Guangye, Hattne, Johan, Hellmich, Julia, Héroux, Annie, Ibrahim, Mohamed, Kern, Jan, Kuczewski, Anthony, Lemke, Henrik T., Liu, Pinghua, Majlof, Lars, McClintock, William M., Myers, Stuart, Nelsen, Silke, Olechno, Joe, Orville, Allen M., Sauter, Nicholas K., Soares, Alexei S., Soltis, S. Michael, Song, Heng, Stearns, Richard G., Tran, Rosalie, Tsai, Yingssu, Uervirojnangkoorn, Monarin, Wilmot, Carrie M., Yachandra, Vittal, Yano, Junko, Yukl, Erik T., Zhu, Diling, Zouni, Athina

“…X-ray free-electron lasers (XFELs) provide very intense X-ray pulses suitable for macromolecular crystallography. Each X-ray pulse typically lasts for tens of…”
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Mechanism of protein oxidative damage that is coupled to long-range electron transfer to high-valent haems by Ma, Zhongxin, Williamson, Heather R, Davidson, Victor L

“…In the absence of its substrate, the auto-reduction of the high-valent bis-Fe(IV) state of the dihaem enzyme MauG is coupled to oxidative damage of a…”
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Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone by Davidson, Victor L, Wilmot, Carrie M

“…Methylamine dehydrogenase (MADH) catalyzes the oxidative deamination of methylamine to formaldehyde and ammonia. Tryptophan tryptophylquinone (TTQ) is the…”
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Structural Determinants of the Specific Activities of an L-Amino Acid Oxidase from Pseudoalteromonas luteoviolacea CPMOR-1 with Broad Substrate Specificity by Mamounis, Kyle J., Caldas Nogueira, Maria Luiza, Marchi Salvador, Daniela Priscila, Andreo-Vidal, Andres, Sanchez-Amat, Antonio, Davidson, Victor L.

“…The Pseudoalteromonas luteoviolacea strain CPMOR-1 expresses a flavin adenine dinucleotide (FAD)-dependent L-amino acid oxidase (LAAO) with broad substrate…”
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Roles of Conserved Residues of the Glycine Oxidase GoxA in Controlling Activity, Cooperativity, Subunit Composition, and Cysteine Tryptophylquinone Biosynthesis by Sehanobish, Esha, Williamson, Heather R., Davidson, Victor L.

“…GoxA is a glycine oxidase that possesses a cysteine tryptophylquinone (CTQ) cofactor that is formed by posttranslational modifications that are catalyzed by a…”
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Cupredoxins--a study of how proteins may evolve to use metals for bioenergetic processes by Choi, Moonsung, Davidson, Victor L

“…Cupredoxins are small proteins that contain type I copper centers, which are ubiquitous in nature. They function as electron transfer shuttles between…”
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Structure and Enzymatic Properties of an Unusual Cysteine Tryptophylquinone-Dependent Glycine Oxidase from Pseudoalteromonas luteoviolacea by Andreo-Vidal, Andres, Mamounis, Kyle J, Sehanobish, Esha, Avalos, Dante, Campillo-Brocal, Jonatan Cristian, Sanchez-Amat, Antonio, Yukl, Erik T, Davidson, Victor L

“…Glycine oxidase from Pseudoalteromonas luteoviolacea (PlGoxA) is a cysteine tryptophylquinone (CTQ)-dependent enzyme. Sequence analysis and phylogenetic…”
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In Crystallo Posttranslational Modification Within a MauG/Pre-Methylamine Dehydrogenase Complex by Jensen, Lyndal M.R, Sanishvili, Ruslan, Davidson, Victor L, Wilmot, Carrie M

“…MauG is a diheme enzyme responsible for the posttranslational modification of two tryptophan residues to form the tryptophan tryptophylquinone (TTQ) cofactor…”
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Converting the bis-FeIV state of the diheme enzyme MauG to Compound I decreases the reorganization energy for electron transfer by Dow, Brian A, Davidson, Victor L

“…The electron transfer (ET) properties of two types of high-valent hemes were studied within the same protein matrix; the bis-Fe(IV) state of MauG and the…”
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Roles of Copper and a Conserved Aspartic Acid in the Autocatalytic Hydroxylation of a Specific Tryptophan Residue during Cysteine Tryptophylquinone Biogenesis by Williamson, Heather R, Sehanobish, Esha, Shiller, Alan M, Sanchez-Amat, Antonio, Davidson, Victor L

“…The first posttranslational modification step in the biosynthesis of the tryptophan-derived quinone cofactors is the autocatalytic hydroxylation of a specific…”
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Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis by Tarboush, Nafez Abu, Jensen, Lyndal M. R, Yukl, Erik T, Geng, Jiafeng, Liu, Aimin, Wilmot, Carrie M, Davidson, Victor L

“…The diheme enzyme MauG catalyzes the posttranslational modification of the precursor protein of methylamine dehydrogenase (preMADH) to complete biosynthesis of…”
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Protein-Derived Cofactors. Expanding the Scope of Post-Translational Modifications by Davidson, Victor L

“…Recent advances in enzymology, structural biology, and protein chemistry have extended the scope of the field of cofactor-dependent enzyme catalysis. It has…”
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Tryptophan tryptophylquinone biosynthesis: A radical approach to posttranslational modification by Davidson, Victor L., Liu, Aimin

“…Protein-derived cofactors are formed by irreversible covalent posttranslational modification of amino acid residues. An example is tryptophan tryptophylquinone…”
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Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis by Yukl, Erik T., Liu, Fange, Krzystek, J., Shin, Sooim, Jensen, Lyndal M. R., Davidson, Victor L., Wilmot, Carrie M., Liu, Aimin

“…Despite the importance of tryptophan (Trp) radicals in biology, very few radicals have been trapped and characterized in a physiologically meaningful context…”
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A Catalytic Di-Heme bis-Fe(IV) Intermediate, Alternative to an Fe(IV)=O Porphyrin Radical by Li, Xianghui, Fu, Rong, Lee, Sheeyong, Krebs, Carsten, Davidson, Victor L., Liu, Aimin

“…High-valent iron species are powerful oxidizing agents in chemical and biological catalysis. The best characterized form of an Fe(V) equivalent described in…”
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Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions by Davidson, Victor L

“…A protein-derived cofactor is a catalytic or redox-active site in a protein that is formed by post-translational modification of one or more amino acid…”
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Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-FeIV state of MauG by Ma, Zhongxin, Williamson, Heather R, Davidson, Victor L

“…The high-valent state of the diheme enzyme MauG exhibits charge-resonance (CR) stabilization in which the major species is a bis-Fe(IV) state with one heme…”
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