Výsledky vyhledávání - "Victor W. T. Cheng"

A conserved lysine residue controls iron–sulfur cluster redox chemistry in Escherichia coli fumarate reductase

Autor: Elena Maklashina, Gary Cecchini, Richard A. Rothery, Victor W. T. Cheng, Quang M. Tran, Joel H. Weiner, Nasim Boroumand

Publikováno v: Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1827:1141-1147

The Escherichia coli respiratory complex II paralogs succinate dehydrogenase (SdhCDAB) and fumarate reductase (FrdABCD) catalyze interconversion of succinate and fumarate coupled to quinone reduction or oxidation, respectively. Based on structural co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::368af5e96e86093fc216310687f7f1b0
https://doi.org/10.1016/j.bbabio.2013.05.004

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Comparative Proteomic and Metabolomic Analysis of Staphylococcus warneri SG1 Cultured in the Presence and Absence of Butanol

Autor: Joel H. Weiner, Yanan Tang, Liang Li, Feifei Fu, Victor W. T. Cheng, Yiman Wu

Publikováno v: Journal of Proteome Research. 12:4478-4489

The complete genome of the solvent tolerant Staphylococcus warneri SG1 was recently published. This Gram-positive bacterium is tolerant to a large spectrum of organic solvents including short-chain alcohols, alkanes, esters and cyclic aromatic compou

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c98b33bb922b7c42b4234036ba50d754
https://doi.org/10.1021/pr400533m

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Redox State of Flavin Adenine Dinucleotide Drives Substrate Binding and Product Release in Escherichia coli Succinate Dehydrogenase

Autor: Elena Maklashina, Gary Cecchini, Richard A. Rothery, Victor W. T. Cheng, Joel H. Weiner, Ramanaguru Siva Piragasam

The Complex II family of enzymes, comprising the respiratory succinate dehydrogenases and fumarate reductases, catalyze reversible interconversion of succinate and fumarate. In contrast to the covalent flavin adenine dinucleotide (FAD) cofactor assem

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c8b5f32464b44871d75f9fa375d0890
https://europepmc.org/articles/PMC4731035/

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The Iron-Sulfur Clusters in Escherichia coli Succinate Dehydrogenase Direct Electron Flow

Autor: Joel H. Weiner, Elysia Ma, Zhongwei Zhao, Victor W. T. Cheng, Richard A. Rothery

Publikováno v: Journal of Biological Chemistry. 281:27662-27668

Succinate dehydrogenase is an indispensable enzyme involved in the Krebs cycle as well as energy coupling in the mitochondria and certain prokaryotes. During catalysis, succinate oxidation is coupled to ubiquinone reduction by an electron transfer re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b54e49edf353c3b416a12ee09a2b9f0
https://doi.org/10.1074/jbc.m604900200

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Investigation of the Environment Surrounding Iron−Sulfur Cluster 4 of Escherichia coli Dimethylsulfoxide Reductase

Autor: Richard Adrian Rothery, Joel H. Weiner, Victor W. T. Cheng, Michela G. Bertero, Natalie C. J. Strynadka

Publikováno v: Biochemistry. 44:8068-8077

Iron-sulfur ([Fe-S]) clusters are common in electron transfer proteins, and their midpoint potentials (E(m) values) play a major role in defining the rate at which electrons are shuttled. The E(m) values of [Fe-S] clusters are largely dependent on th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4de805bd73c7d947c7b2b7b17e2e3ccb
https://doi.org/10.1021/bi050362p

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Complete Genome of the Solvent-Tolerant Staphylococcus warneri Strain SG1

Autor: Doug Ridgway, Michael J. Ellison, Joel H. Weiner, Victor W. T. Cheng, Guijin Zhang, Kayode S. Oyedotun

Publikováno v: Genome Announcements

Staphylococcus warneri is a Gram-positive bacterium commonly found in human skin flora. The genome of a laboratory S. warneri isolate, strain SG1, was sequenced to explore its mechanism of solvent tolerance and its potential as a chassis for biofuel

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41f6dd2fc8466bdda721138a9200ec59
http://europepmc.org/articles/PMC3622959

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Alternative sites for proton entry from the cytoplasm to the quinone binding site in Escherichia coli succinate dehydrogenase

Autor: Richard A. Rothery, Victor W. T. Cheng, Joel H. Weiner, Antonia Johnson

Publikováno v: Biochemistry. 47(35)

Escherichia coli succinate dehydrogenase (Sdh) belongs to the highly conserved complex II family of enzymes that reduce ubiquinone. These enzymes do not generate a protonmotive force during catalysis and are electroneutral. Because of its electroneut

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f616e49213e359e286720381a6f8b7c7
https://pubmed.ncbi.nlm.nih.gov/18690748

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