Relating diffusion along the substrate tunnel and oxygen sensitivity in hydrogenase.
about
Crystallographic studies of [NiFe]-hydrogenase mutants: towards consensus structures for the elusive unready oxidized states[NiFe]-hydrogenases revisited: nickel-carboxamido bond formation in a variant with accrued O2-tolerance and a tentative re-interpretation of Ni-SI statesDesign and development of synthetic microbial platform cells for bioenergyReversible oxygen-tolerant hydrogenase carried by free-living N2-fixing bacteria isolated from the rhizospheres of rice, maize, and wheatA threonine stabilizes the NiC and NiR catalytic intermediates of [NiFe]-hydrogenase.Control of the Position of Oxygen Delivery in Soybean Lipoxygenase-1 by Amino Acid Side Chains within a Gas Migration ChannelInfluence of the protein structure surrounding the active site on the catalytic activity of [NiFeSe] hydrogenases.A cell-free microtiter plate screen for improved [FeFe] hydrogenases.Aerobic damage to [FeFe]-hydrogenases: activation barriers for the chemical attachment of O2.A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianumAnalyses of the large subunit histidine-rich motif expose an alternative proton transfer pathway in [NiFe] hydrogenases.[FeFe]-hydrogenase abundance and diversity along a vertical redox gradient in Great Salt Lake, USA.Engineering photosynthetic organisms for the production of biohydrogen.Regioselectivity of H cluster oxidation.Mechanistic insight into the blocking of CO diffusion in [NiFe]-hydrogenase mutants through multiscale simulation.Relation between anaerobic inactivation and oxygen tolerance in a large series of NiFe hydrogenase mutants.Molecular evolution of gas cavity in [NiFeSe] hydrogenases resurrected in silicoOxygen tolerance of an in silico-designed bioinspired hydrogen-evolving catalyst in water.Gates of enzymes.All the O2 Consumed by Thermus thermophilus Cytochrome ba3 Is Delivered to the Active Site through a Long, Open Hydrophobic Tunnel with Entrances within the Lipid Bilayer.Enzymes as modular catalysts for redox half-reactions in H2-powered chemical synthesis: from biology to technology.The quest for a functional substrate access tunnel in FeFe hydrogenase.Structure, function and biosynthesis of O₂-tolerant hydrogenases.Enhanced oxygen-tolerance of the full heterotrimeric membrane-bound [NiFe]-hydrogenase of Ralstonia eutropha.Carbon monoxide as an electron donor for the biological reduction of sulphateH₂-dependent azoreduction by Shewanella oneidensis MR-1: involvement of secreted flavins and both [Ni-Fe] and [Fe-Fe] hydrogenases.Kinetics and thermodynamics of gas diffusion in a NiFe hydrogenase.Mechanism of O2 diffusion and reduction in FeFe hydrogenases.Protein Electrochemistry: Questions and Answers.Role of an N-terminal extension in stability and catalytic activity of a hyperthermostable α/β hydrolase fold esterase.Theoretical investigation of aerobic and anaerobic oxidative inactivation of the [NiFe]-hydrogenase active site.Tracking the route of molecular oxygen in O2-tolerant membrane-bound [NiFe] hydrogenase.The mechanism of inhibition by H2 of H2-evolution by hydrogenases.Development of an infrared spectroscopic approach for studying metalloenzyme active site chemistry under direct electrochemical control.
P2860
Q27695711-4E0DAFF3-0CE4-484B-9AAC-6E473393C8E4Q27698514-707E6BAB-85C1-4BA3-AC63-E5CD70867C06Q28708939-B9193FC5-7B4C-42A7-8588-EEF2378A7608Q28710124-5ACF8EF9-8505-493F-8C5C-67A796EFC71BQ30371600-947692A5-7C76-4179-92D6-34C54116AAFDQ30384353-812A55A4-D406-40C8-83BA-E111F19CE73EQ30427940-6E24E4AA-DBE8-43C9-8C9B-0FAFE9194B1EQ30982726-A2DC0DA6-88EF-420B-A199-84FDBC9C37C7Q34083234-0BF1E005-446C-4908-A380-FD0B175FA55BQ34169576-2E0CB8B0-8E81-46FE-B6BA-1844A151D144Q34214342-71F1F130-6028-46F1-9710-B7DE6FB49F8FQ34236840-11ED0BF0-3A7C-42A3-B045-7A161C24DAB3Q34833832-F45E3053-1B62-4990-B3CE-763006A83419Q35092606-6B0A3BF4-6645-499F-BAFD-AFEF3FE7025CQ35615181-AB3A209D-BB77-4781-80DC-7074415B43D4Q35921991-CF74DC98-3418-4E23-94EB-D8C39DA59C8FQ36471139-D65EF1DD-D744-4FB4-A483-1E9F6BEFE7D4Q36511970-39538194-7653-4446-B35C-BE368268C6CAQ36598197-E05480ED-95A7-4E45-BCE5-5B5731D84563Q37098498-F2CC5C7E-870E-437E-AEA3-C33B1B6F4534Q37481801-A0DFD3DB-B8D6-4FB0-89C3-5D556CAC0897Q37632855-2FBED9E2-BB64-4CB3-BFAD-D65E9A2ADD9CQ37842302-C404F8A4-BA6A-4659-90B8-EFBC9FDF9139Q38074265-88B884A5-8E6D-4E89-9F6C-B5EC3C56CDFEQ41387381-E6A99715-40B7-47BF-BC65-A5B52E81CA25Q42091019-A27FA179-D48E-4D90-B016-C6C4CF3A83A2Q45391937-FEF7FA03-4ACD-41B7-A41E-C5D2F2256FC4Q46068436-58758761-FC7C-495F-8E98-176FBF31DAC0Q46442968-9F1DC2D5-453A-4C2B-9EE5-155F12029936Q46489390-0064366E-57E4-40F7-A3C4-4CB2051125BDQ47716456-AC53B0AF-4C9B-4829-A805-6B77607E63B2Q49631041-918181B6-E85B-4BE5-B051-D56FB4C03E24Q49790531-2A2F442C-B445-4D8E-89B4-7B8348F93745Q50885079-D7B85527-116E-4420-AA93-0E6431ECF8EEQ53438242-96A69288-A225-435B-AE82-75A85C04DEE9
P2860
Relating diffusion along the substrate tunnel and oxygen sensitivity in hydrogenase.
description
2009 nî lūn-bûn
@nan
2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Relating diffusion along the substrate tunnel and oxygen sensitivity in hydrogenase.
@ast
Relating diffusion along the substrate tunnel and oxygen sensitivity in hydrogenase.
@en
type
label
Relating diffusion along the substrate tunnel and oxygen sensitivity in hydrogenase.
@ast
Relating diffusion along the substrate tunnel and oxygen sensitivity in hydrogenase.
@en
prefLabel
Relating diffusion along the substrate tunnel and oxygen sensitivity in hydrogenase.
@ast
Relating diffusion along the substrate tunnel and oxygen sensitivity in hydrogenase.
@en
P2093
P50
P356
P1476
Relating diffusion along the substrate tunnel and oxygen sensitivity in hydrogenase
@en
P2093
Bruno Guigliarelli
Bénédicte Burlat
Carole Baffert
Christine Cavazza
Fanny Leroux
Isabelle Meynial-Salles
Juan Carlos Fontecilla-Camps
Marc Rousset
Patrick Bertrand
Philippe Soucaille
P2888
P356
10.1038/NCHEMBIO.276
P577
2009-12-06T00:00:00Z