Structure of Alcaligenes faecalis nitrite reductase and a copper site mutant, M150E, that contains zinc
about
Protein design: toward functional metalloenzymesCatalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of copper-containing nitrite reductasepH dependence of copper geometry, reduction potential, and nitrite affinity in nitrite reductaseCrystal Structure of a Two-domain Multicopper Oxidase: IMPLICATIONS FOR THE EVOLUTION OF MULTICOPPER BLUE PROTEINSStructure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implicationsCatalytic and spectroscopic analysis of blue copper-containing nitrite reductase mutants altered in the environment of the type 2 copper centre: implications for substrate interactionAtomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanismA random-sequential mechanism for nitrite binding and active site reduction in copper-containing nitrite reductase.Binding and activation of nitrite and nitric oxide by copper nitrite reductase and corresponding model complexes.The extended environment of mononuclear metal centers in protein structuresRecent structural insights into the function of copper nitrite reductases.Nitrous oxide production by Alcaligenes faecalis under transient and dynamic aerobic and anaerobic conditions.Structural comparison of cupredoxin domains: domain recycling to construct proteins with novel functions.Site-directed mutations in fungal laccase: effect on redox potential, activity and pH profile.Ligand-exchange processes on solvated zinc cations: water exchange on [Zn(H2O)4(L)]2+.2H2O (L=heterocyclic ligand).Dithionite reduction kinetics of the dissimilatory copper-containing nitrite reductase of Alcalegenes xylosoxidans. The SO(2)(.-) radical binds to the substrate binding type 2 copper site before the type 2 copper is reduced.
P2860
Q26866201-D1A4681A-1C86-4189-93B2-3499A184E0C9Q27622541-A27614C1-4301-4FD4-A69E-5BB5F0A188F7Q27643214-9F570B33-9CA5-49BC-BE0F-CDCC0C78C5DAQ27653839-63D99E01-83AD-425C-9916-7E9771074595Q27746733-2F978539-05DA-4969-B21E-08F15C76F204Q28345522-F5A3495A-7E9F-44CA-96D5-A75C43BED42AQ33922878-F69B8F7C-BADE-48FF-B0CE-8A59BB709F30Q34566514-78684E8C-3ABA-494C-A810-68C59142FCC2Q34632334-F098CAEF-F1C6-4997-AB7F-311E82129341Q36800992-703FD498-338D-4DD4-810F-6FB3A650B906Q39431953-1AB52229-0B20-40D6-84AA-8670AC62C40FQ39800091-FF893822-3C52-4D42-9431-C07A54ED9A66Q41858464-72573856-5D3C-4E1B-A654-2383E79582ADQ42991416-FCA77DCC-8893-4A36-9971-3A0FAF3A295DQ43063650-C5BDA72D-BB2E-4711-8198-F434D1CC2063Q50499615-3B5D9BC5-19E2-4B6D-9F7E-7198D3B78B8F
P2860
Structure of Alcaligenes faecalis nitrite reductase and a copper site mutant, M150E, that contains zinc
description
1995 nî lūn-bûn
@nan
1995 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Structure of Alcaligenes faeca ...... ant, M150E, that contains zinc
@ast
Structure of Alcaligenes faeca ...... ant, M150E, that contains zinc
@en
Structure of Alcaligenes faeca ...... ant, M150E, that contains zinc
@nl
type
label
Structure of Alcaligenes faeca ...... ant, M150E, that contains zinc
@ast
Structure of Alcaligenes faeca ...... ant, M150E, that contains zinc
@en
Structure of Alcaligenes faeca ...... ant, M150E, that contains zinc
@nl
prefLabel
Structure of Alcaligenes faeca ...... ant, M150E, that contains zinc
@ast
Structure of Alcaligenes faeca ...... ant, M150E, that contains zinc
@en
Structure of Alcaligenes faeca ...... ant, M150E, that contains zinc
@nl
P2093
P356
P1433
P1476
Structure of Alcaligenes faeca ...... ant, M150E, that contains zinc
@en
P2093
M E Murphy
M Kukimoto
M Nishiyama
M Tanokura
S Horinouchi
P304
P356
10.1021/BI00038A003
P407
P577
1995-09-26T00:00:00Z