Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: [Fe-S] cluster-driven protein rearrangement
about
Alteration of the reduction potential of the [4Fe-4S](2+/+) cluster of Azotobacter vinelandii ferredoxin IStructure of C42D Azotobacter vinelandii FdI. A Cys-X-X-Asp-X-X-Cys motif ligates an air-stable [4Fe-4S]2+/+ clusterAzotobacter vinelandii ferredoxin I: a sequence and structure comparison approach to alteration of [4Fe-4S]2+/+ reduction potentialSite-directed mutagenesis of Azotobacter vinelandii ferredoxin I: cysteine ligation of the [4Fe-4S] cluster with protein rearrangement is preferred over serine ligationConstruction of a bisaquo heme enzyme and binding by exogenous ligandsY13C Azotobacter vinelandii ferredoxin I. A designed [Fe-S] ligand motif contains a cysteine persulfideA T14C variant of Azotobacter vinelandii ferredoxin I undergoes facile [3Fe-4S]0 to [4Fe-4S]2+ conversion in vitro but not in vivoVariations on a (t)heme--novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamilyThe hydrogenase cytochrome b heme ligands of Azotobacter vinelandii are required for full H(2) oxidation capability.Role of aromatic residues in stabilization of the [Fe4S4] cluster in high-potential iron proteins (HiPIPs): physical characterization and stability studies of Tyr-19 mutants of Chromatium vinosum HiPIP.Asp1 from Schizosaccharomyces pombe binds a [2Fe-2S](2+) cluster which inhibits inositol pyrophosphate 1-phosphatase activityThe genes encoding the delta subunits of dinitrogenases 2 and 3 are required for mo-independent diazotrophic growth by Azotobacter vinelandii.In Azotobacter vinelandii hydrogenase, substitution of serine for the cysteine residues at positions 62, 65, 294, and 297 in the small (HoxK) subunit affects H2 oxidation [corrected]Purification and biophysical characterization of a new [2Fe-2S] ferredoxin from Azotobacter vinelandii, a putative [Fe-S] cluster assembly/repair protein.Altered nitrogenase MoFe proteins from Azotobacter vinelandii. Analysis of MoFe proteins having amino acid substitutions for the conserved cysteine residues within the beta-subunitMolecular characterization of human xanthine oxidoreductase: the enzyme is grossly deficient in molybdenum and substantially deficient in iron-sulphur centresA new type 2 copper cysteinate azurin. Involvement of an engineered exposed cysteine in copper binding through internal rearrangement.Iron-sulfur cluster N2 of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is located on subunit NuoB.Discovery and characterization of a prevalent human gut bacterial enzyme sufficient for the inactivation of a family of plant toxins.
P2860
Q27620642-7723A2CA-2D73-4244-BF34-660F285BAF8EQ27626713-D1494F4E-8E77-4DE3-B2A7-FECC137CFE9CQ27636135-6CF0F542-59B6-470E-A367-4BC7A35BE01AQ27729295-A1EA7668-F706-4080-80C3-4BECD4E7E995Q27730310-5BFF73EF-B635-4A96-B881-429FAE1C92BDQ27739255-B68966AA-6C1E-489D-BCFA-8B96962F1E21Q27766116-FBF704D3-9842-4780-AC97-6FC497FACFE9Q28304165-E1A423E2-1A5A-49F5-90EF-8780C2257F0AQ33602585-4F09EAC4-5752-4755-A172-2B93EDD1EC30Q33845598-9F80D8F3-4C96-416D-86A3-9660FF5621FCQ36270671-F29AD3B7-19B7-47DF-B421-7F0934381449Q39836009-0A702FEB-01AF-4DBE-ADF9-E995CFAA07D2Q39928894-9015C7EB-5A12-4C75-A35A-ED286705F71BQ41699478-0669F1F8-F762-4439-8C25-2E822EB43E50Q42099196-77C73615-FD52-4DDF-8DB9-10B9A7A3AEA8Q42836829-D368C2FC-D78D-4C73-A423-8715BD19E20DQ44108461-B9AA8145-0B4D-4737-BF0E-B99ABE42DE23Q44585471-4CB98608-C66B-4AF6-9D9D-1B02C9133C55Q55375238-800EB3F6-A19B-4670-A735-B663D0C21662
P2860
Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: [Fe-S] cluster-driven protein rearrangement
description
1990 nî lūn-bûn
@nan
1990 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Site-directed mutagenesis of A ...... r-driven protein rearrangement
@ast
Site-directed mutagenesis of A ...... r-driven protein rearrangement
@en
Site-directed mutagenesis of A ...... r-driven protein rearrangement
@nl
type
label
Site-directed mutagenesis of A ...... r-driven protein rearrangement
@ast
Site-directed mutagenesis of A ...... r-driven protein rearrangement
@en
Site-directed mutagenesis of A ...... r-driven protein rearrangement
@nl
prefLabel
Site-directed mutagenesis of A ...... r-driven protein rearrangement
@ast
Site-directed mutagenesis of A ...... r-driven protein rearrangement
@en
Site-directed mutagenesis of A ...... r-driven protein rearrangement
@nl
P2093
P2860
P356
P1476
Site-directed mutagenesis of A ...... r-driven protein rearrangement
@en
P2093
A E Martín
B K Burgess
G M Jensen
P J Stephens
P2860
P304
P356
10.1073/PNAS.87.2.598
P407
P577
1990-01-01T00:00:00Z