Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I
about
QM/MM molecular dynamics studies of metal binding proteinsProbing the conformational mobility of the active site of a heme peroxidaseCrystal structures of cyanide- and triiodide-bound forms of Arthromyces ramosus peroxidase at different pH values. Perturbations of active site residues and their implication in enzyme catalysisStructure of barley grain peroxidase refined at 1.9-A resolution. A plant peroxidase reversibly inactivated at neutral pHEffects of the location of distal histidine in the reaction of myoglobin with hydrogen peroxideEffect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: mutations near the high-affinity cytochrome c binding site.Reduction potential of yeast cytochrome c peroxidase and three distal histidine mutants: dependence on pHCrystal structure of Mycobacterium tuberculosis catalase-peroxidaseSubstrate, product, and cofactor: The extraordinarily flexible relationship between the CDE superfamily and hemeProbing the active site residues in aromatic donor oxidation in horseradish peroxidase: involvement of an arginine and a tyrosine residue in aromatic donor bindingKinetic and spectroscopic characterization of a hydroperoxy compound in the reaction of native myoglobin with hydrogen peroxide.The chlorite dismutase (HemQ) from Staphylococcus aureus has a redox-sensitive heme and is associated with the small colony variant phenotype.Heme enzyme structure and function.Peroxidase-type reactions suggest a heterolytic/nucleophilic O-O joining mechanism in the heme-dependent chlorite dismutase.Effect of active site and surface mutations on the reduction potential of yeast cytochrome c peroxidase and spectroscopic properties of the oxidized and reduced enzyme.Apolar distal pocket mutants of yeast cytochrome c peroxidase: hydrogen peroxide reactivity and cyanide binding of the TriAla, TriVal, and TriLeu variants.Characterization of four covalently-linked yeast cytochrome c/cytochrome c peroxidase complexes: Evidence for electrostatic interaction between bound cytochrome c molecules.Unusual Peroxide-Dependent, Heme-Transforming Reaction Catalyzed by HemQ.Production of dioxygen in the dark: dismutases of oxyanions.Kinetic and equilibrium studies of acrylonitrile binding to cytochrome c peroxidase and oxidation of acrylonitrile by cytochrome c peroxidase compound I.Thirty years of heme peroxidase structural biology.Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis.The HemQ coprohaem decarboxylase generates reactive oxygen species: implications for the evolution of classical haem biosynthesis.Activation of hydrogen peroxide in horseradish peroxidase occurs within approximately 200 micro s observed by a new freeze-quench device.Rescue of His-42 --> Ala horseradish peroxidase by a Phe-41 --> His mutation. Engineering of a surrogate catalytic histidine.Horseradish peroxidase His-42 --> Ala, His-42 --> Val, and Phe-41 --> Ala mutants. Histidine catalysis and control of substrate access to the heme iron.Mechanism-based inactivation of lacrimal-gland peroxidase by phenylhydrazine: a suicidal substrate to probe the active site.Effect of alternative distal residues on the reactivity of cytochrome c peroxidase: properties of CcP mutants H52D, H52E, H52N, and H52Q.LC-MS/MS suggests that hole hopping in cytochrome c peroxidase protects its heme from oxidative modification by excess H2O2.Leishmania major encodes an unusual peroxidase that is a close homologue of plant ascorbate peroxidase: a novel role of the transmembrane domain.Mutational analysis of the role of the distal histidine and glutamine residues of prostaglandin-endoperoxide synthase-2 in peroxidase catalysis, hydroperoxide reduction, and cyclooxygenase activation.Binding of imidazole, 1-methylimidazole and 4-nitroimidazole to yeast cytochrome c peroxidase (CcP) and the distal histidine mutant, CcP(H52L).Reaction of variant sperm-whale myoglobins with hydrogen peroxide: the effects of mutating a histidine residue in the haem distal pocket.Role of histidine 42 in ascorbate peroxidase. Kinetic analysis of the H42A and H42E variants.Examining the role of glutamic acid 183 in chloroperoxidase catalysis.Crystal structure and functional analysis of Leishmania major pseudoperoxidase.Absence of a detectable intermediate in the compound I formation of horseradish peroxidase at ambient temperature.On the relationship of coral allene oxide synthase to catalase. A single active site mutation that induces catalase activity in coral allene oxide synthase.Roles of distal aspartate and arginine of B-class dye-decolorizing peroxidase in heterolytic hydrogen peroxide cleavageEffect of Distal Cavity Mutations on the Formation of Compound I in Catalase-Peroxidases
P2860
Q26823476-E51C318F-FC8A-4E91-A6C2-B3F54364880AQ27683530-78103EF9-F46A-48EA-BB00-231D5D530574Q27729886-2952EE1B-D6BD-4BAB-B5CE-B4868D5B73DBQ27748820-D1A5BCE2-8102-4185-A4CC-7F644A509637Q27766717-731CA6A0-D02D-43C3-BED6-6369F81975E0Q27930007-D07E2377-B89E-47A0-A4E1-16DAD1764DE8Q27937848-78C66CE3-5670-4957-9F83-1EBFC5C5DDE0Q28487119-5B584F8B-F7A5-4CF5-8777-2FDA804644EBQ30152968-FDF10E8D-FE06-4444-9BEB-563AA5C5B92AQ30423738-D7F2BCBD-C02A-464D-843E-EEF188A40C40Q30816618-2FC504E0-5CD3-424B-9256-C07B3B54C9FDQ33573978-27991ADA-81E3-4EFA-8F59-F4D9A3D0383FQ34396417-EE473CFD-7573-4FC9-8F3C-4A0C6EE641F9Q35323100-2FD169BE-A703-44C7-9552-04427D1E59A7Q35933918-5E0973C6-BD6F-42F1-AF1B-79261E93A55CQ36489825-5E181EB7-93B8-4D31-8DFE-EFC62510FDEBQ36914548-241A42BF-4A94-41D7-93D6-3B20355A380BQ37107616-BED5A2C7-7EDF-4F1E-8031-1AAC81D0B666Q37234797-32FD3CA0-4545-4F4F-B4F3-276C163B2DE3Q37497862-C795154E-DDE2-4330-8AD0-FCB9BBEED68FQ37703495-42DECFA1-3912-42DB-B0FB-10ABD88B103BQ38361435-C9775F12-6D1C-4ED5-A8EC-BECB01F8E598Q39420526-9116EEE2-D2DC-4074-BDC8-B2DEA971C5F4Q40232318-988B3986-A774-40A9-BCA0-CA710CC2F82EQ41159715-D80D550F-8F5F-4A79-8C0A-2A9645F3C097Q41310167-29B4F3BA-0F40-4E54-89BA-55D600AF1684Q41834816-68299D87-4C54-4611-9A64-373F5325B030Q41877947-751ACF48-F039-41F7-841D-6D041EF3EED3Q41965338-7CE4FCFB-84BA-4325-9388-E359FABE0771Q42050429-DF28EE2F-F790-46F5-8DE7-8FB263BC4121Q42061810-287FF0D0-EFE7-4A71-AB15-5769A351B711Q42563506-4DA05B71-8FB9-4E46-9802-69C653B54D86Q42987459-AC51A0FB-6DA5-4AB0-9476-B698F3DCD0E4Q44041393-641B535C-4529-4AC8-B408-75C246274C21Q44308479-E182C1BC-36B4-4A4E-AB26-81A8962CB70AQ46315893-5E76662F-B26E-486D-9A2A-A3FF892E0122Q46749941-D0111D44-026C-4927-AA66-F204F5B09C6FQ46972982-CEA4FEC1-3C5C-4A13-980C-EB95DF4CE55BQ58802667-5C1A4E58-B352-4CA8-893E-AF071619AB95Q59053748-91054195-6000-4C36-AF6C-7F1731EDC5AE
P2860
Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I
description
1993 nî lūn-bûn
@nan
1993 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Histidine 52 is a critical res ...... chrome c peroxidase compound I
@ast
Histidine 52 is a critical res ...... chrome c peroxidase compound I
@en
Histidine 52 is a critical res ...... chrome c peroxidase compound I
@nl
type
label
Histidine 52 is a critical res ...... chrome c peroxidase compound I
@ast
Histidine 52 is a critical res ...... chrome c peroxidase compound I
@en
Histidine 52 is a critical res ...... chrome c peroxidase compound I
@nl
prefLabel
Histidine 52 is a critical res ...... chrome c peroxidase compound I
@ast
Histidine 52 is a critical res ...... chrome c peroxidase compound I
@en
Histidine 52 is a critical res ...... chrome c peroxidase compound I
@nl
P2093
P3181
P356
P1433
P1476
Histidine 52 is a critical res ...... chrome c peroxidase compound I
@en
P2093
P304
P3181
P356
10.1021/BI00088A035
P407
P577
1993-09-21T00:00:00Z