about
Single Enzyme Experiments Reveal a Long-Lifetime Proton Leak State in a Heme-Copper OxidaseRegulatory role of the respiratory supercomplex factors in Saccharomyces cerevisiaeCopper-Oxygen Complexes Revisited: Structures, Spectroscopy, and Reactivity.A Designed Metalloenzyme Achieving the Catalytic Rate of a Native Enzyme.Electrocatalytic O2-Reduction by Synthetic Cytochrome c Oxidase Mimics: Identification of a "Bridging Peroxo" Intermediate Involved in Facile 4e(-)/4H(+) O2-Reduction.Functional and structural evaluation of bovine heart cytochrome c oxidase incorporated into bicelles.Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.Synthetic heme/copper assemblies: toward an understanding of cytochrome c oxidase interactions with dioxygen and nitrogen oxides.Ru(II)-diimine functionalized metalloproteins: From electron transfer studies to light-driven biocatalysis.Delipidation of cytochrome c oxidase from Rhodobacter sphaeroides destabilizes its quaternary structure.Peroxo and Superoxo Moieties Bound to Copper Ion: Electron-Transfer Equilibrium with a Small Reorganization Energy.Dimer interface of bovine cytochrome c oxidase is influenced by local posttranslational modifications and lipid binding.Heme isomers substantially affect heme's electronic structure and function.Probing biological redox chemistry with large amplitude Fourier transformed ac voltammetry.Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature.The dual function of flavodiiron proteins: oxygen and/or nitric oxide reductases.Reactivity of the copper(iii)-hydroxide unit with phenols.Activation of dioxygen by copper metalloproteins and insights from model complexes.Energetic Mechanism of Cytochrome c-Cytochrome c Oxidase Electron Transfer Complex Formation under Turnover Conditions Revealed by Mutational Effects and Docking Simulation.Deciphering a 20-Year-Old Conundrum: The Mechanisms of Reduction by the Water/Amine/SmI2 Mixture.Structure of bovine cytochrome c oxidase crystallized at a neutral pH using a fluorinated detergentA nanosecond time-resolved XFEL analysis of structural changes associated with CO release from cytochrome c oxidase.Water exit pathways and proton pumping mechanism in B-type cytochrome c oxidase from molecular dynamics simulations.Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme.The cellular membrane as a mediator for small molecule interaction with membrane proteins.A broken-symmetry density functional study of structures, energies, and protonation states along the catalytic O-O bond cleavage pathway in ba3 cytochrome c oxidase from Thermus thermophilus.Two-dimensional crystallization of monomeric bovine cytochrome c oxidase with bound cytochrome c in reconstituted lipid membranesComplex structure of cytochrome c-cytochrome c oxidase reveals a novel protein-protein interaction mode.Phenol-Induced O-O Bond Cleavage in a Low-Spin Heme-Peroxo-Copper Complex: Implications for O2 Reduction in Heme-Copper Oxidases.Manganese and Cobalt in the Nonheme-Metal-Binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-Inactive Mechanism.Critical Aspects of Heme-Peroxo-Cu Complex Structure and Nature of Proton Source Dictate Metal-O(peroxo) Breakage versus Reductive O-O Cleavage Chemistry.Dinuclear Complexes Formed by Hydrogen Bonds: Synthesis, Structure and Magnetic and Electrochemical Properties.Probing the nitrite and nitric oxide reductase activity of cbb3 oxidase: resonance Raman detection of a six-coordinate ferrous heme-nitrosyl species in the binuclear b3/CuB center.The Mg2+-containing Water Cluster of Mammalian Cytochrome c Oxidase Collects Four Pumping Proton Equivalents in Each Catalytic Cycle.Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.Insights into functions of the H channel of cytochrome c oxidase from atomistic molecular dynamics simulations.Electrochemistry of Metalloproteins Attached through Functional Self-Assembled Monolayers on Gold and Ferromagnetic Electrodes.Chemical Biology of H2S Signaling through Persulfidation.The reductive phase of Rhodobacter sphaeroides cytochrome c oxidase disentangled by CO ligation.Structures of the Heme Acquisition Protein HasA with Iron(III)-5,15-Diphenylporphyrin and Derivatives Thereof as an Artificial Prosthetic Group.
P2860
Q27336338-C2305125-90D1-4B4B-B85B-9F52F24448B9Q30268460-095934CA-83BD-4C96-927D-D68C6FB1E058Q36253692-9F1DD335-A778-4F1F-8AD6-985F167F9835Q36364991-343EEA14-DE44-44C1-BE24-F731BA68696CQ36402420-75E1679D-9383-4B0F-824D-B2E6043E034EQ36494318-1F7C985B-A3B8-4A80-AF9B-8C7350E3045CQ36601149-F489278F-F340-4B66-B549-E363F113E93BQ36654671-D3F985AA-8058-49DE-AB8C-E15999C060ACQ36731016-3E351F3E-F2C0-44BE-9B32-ECE262928BE7Q36901556-8BC2D5AF-6D82-41D8-A29C-01D487DBDB2CQ37108684-1F9F874A-538D-4F64-8A9B-59A7E0BE69C2Q37126703-D2AA2C3C-5C98-486F-98F0-E6DB2ECD0452Q38626338-83EF4BD9-F942-4E64-8ED9-68D53715EDFAQ38626511-74AD9AF8-2BE7-40A9-8C0A-6B1C8A58F412Q38683342-C214D295-E112-417D-8AB9-4C6536DEB9A0Q38696686-247E0400-BC37-4364-8D02-3311FD4C24B5Q38749805-CAC13FD4-FBC7-4C02-895F-390831840BE4Q39030299-DBBBAC97-894D-4B79-BB6F-0D231DE308C1Q39735331-A443974B-67F6-4216-8664-489680EF7004Q40366042-63A0E69B-0A44-48D5-AD34-57AC98BE23B3Q40981550-E335F73B-E282-486B-BAAA-FAB817D002E3Q41018261-CE15E37C-D21C-4E93-95E6-D26E34D6A9CEQ41349037-318C5E35-C6B5-486C-A2FC-71688853EA70Q41527531-AA1FCF0D-0864-4F81-8598-DD4F929F503BQ41633843-9545CA64-D38D-4158-85A8-1728FC8765ADQ41842908-59674895-8CD4-42E6-B866-48E7E5420215Q42081079-1DD98BF6-6E24-4073-B542-3F680A6628E4Q42325134-A0BEC2D8-4DA1-4E09-948B-27BA06789A08Q46188634-DA5205BB-DA94-43F3-98B3-E9FA73645C59Q46327151-4883C4B1-F841-4691-924D-C68DE9AF5A40Q46342369-AE5F4DB4-10D4-4107-8B38-8CF91EDD7AB4Q46401864-1A2D6BBA-4A09-4AE4-BC53-8F249B131757Q46654695-E93EDFFD-3CF7-4D5A-A061-1F95DC0C1034Q47146027-994DEC7E-E605-48E6-861E-1022520F4C42Q47245449-967EEF90-6BDF-4F76-B47E-6D7DFF07424FQ47407220-E883FE64-C771-4960-AE4D-867C5AA7FA9CQ47417571-BC24B6AD-CABA-4671-A913-2806DC7E9A1CQ47430972-34352DAB-C9AC-4700-B422-DC78BFA9A587Q47607396-7247B0D0-4109-4A09-86A4-91F7A4CBD170Q47663874-D4578331-23A8-444D-8428-585293422B97
P2860
description
2015 nî lūn-bûn
@nan
2015 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
Reaction mechanism of cytochrome c oxidase.
@ast
Reaction mechanism of cytochrome c oxidase.
@en
Reaction mechanism of cytochrome c oxidase.
@nl
type
label
Reaction mechanism of cytochrome c oxidase.
@ast
Reaction mechanism of cytochrome c oxidase.
@en
Reaction mechanism of cytochrome c oxidase.
@nl
prefLabel
Reaction mechanism of cytochrome c oxidase.
@ast
Reaction mechanism of cytochrome c oxidase.
@en
Reaction mechanism of cytochrome c oxidase.
@nl
P356
P1433
P1476
Reaction mechanism of cytochrome c oxidase.
@en
P2093
Atsuhiro Shimada
Shinya Yoshikawa
P304
P356
10.1021/CR500266A
P577
2015-01-20T00:00:00Z