An engineered two-iron superoxide reductase lacking the [Fe(SCys)4] site retains its catalytic properties in vitro and in vivo.
about
Desulfoferrodoxin of Clostridium acetobutylicum functions as a superoxide reductaseBiological inorganic chemistry at the beginning of the 21st century.Superoxide dismutases and superoxide reductases.Treponema denticola superoxide reductase: in vivo role, in vitro reactivities, and a novel [Fe(Cys)(4)] siteGeometries and electronic structures of cyanide adducts of the non-heme iron active site of superoxide reductases: vibrational and ENDOR studiesSulfur K-edge X-ray absorption spectroscopy and density functional theory calculations on superoxide reductase: role of the axial thiolate in reactivityMetalloproteins containing cytochrome, iron-sulfur, or copper redox centersPurification, crystallization and X-ray crystallographic analysis of Archaeoglobus fulgidus neelaredoxin.Reductive activation and structural rearrangement in superoxide reductase: a combined infrared spectroscopic and computational study.Kinetics of the superoxide reductase catalytic cycle.Structural Characterization of Ferrous Ion Binding to Retinal Guanylate Cyclase Activator Protein 5 from Zebrafish Photoreceptors.Domain motions and electron transfer dynamics in 2Fe-superoxide reductase.Intermolecular electron transfer in two-iron superoxide reductase: a putative role for the desulforedoxin center as an electron donor to the iron active site.Dimerization of Neuronal Calcium Sensor Proteins
P2860
Q28485881-5F9A0721-2C9F-428B-B0B4-09864DE125F8Q34913839-4DB02FEA-8FA1-4AEB-8752-2D6001EC5FE5Q35049047-03610A37-FD09-44A2-9255-0AA5E10475A8Q36249941-562B1679-6C5C-4B5F-8806-3140350FCC7AQ36865938-F196BAF7-EB81-465F-8F13-52562C62D392Q36869531-1A20BD78-09C9-4AB2-8300-39946BCD5FAAQ37727718-4A6BC7A2-5163-4B78-9118-F4F62B3421D8Q39433705-218D9685-9E48-4621-8E96-BE80CFBED929Q44355215-664B58A9-169B-458A-9863-42515AABB310Q44538211-856F93F1-8559-4679-8045-78FEF904E4F7Q46063568-2015228F-218F-4ABA-ADB8-FAE73B88D54BQ46506208-DE22905C-0C5C-4D34-BDE3-F001F7BC570DQ54361176-5EA12657-46E7-43B2-A406-D1C722125E35Q59137482-63D26242-CDE0-4BE5-9289-6C00FD5D4061
P2860
An engineered two-iron superoxide reductase lacking the [Fe(SCys)4] site retains its catalytic properties in vitro and in vivo.
description
2003 nî lūn-bûn
@nan
2003 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մարտին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
An engineered two-iron superoxide reductase lacking the [Fe
@nl
An engineered two-iron superox ...... operties in vitro and in vivo.
@ast
An engineered two-iron superox ...... operties in vitro and in vivo.
@en
type
label
An engineered two-iron superoxide reductase lacking the [Fe
@nl
An engineered two-iron superox ...... operties in vitro and in vivo.
@ast
An engineered two-iron superox ...... operties in vitro and in vivo.
@en
prefLabel
An engineered two-iron superoxide reductase lacking the [Fe
@nl
An engineered two-iron superox ...... operties in vitro and in vivo.
@ast
An engineered two-iron superox ...... operties in vitro and in vivo.
@en
P2093
P2860
P356
P1476
An engineered two-iron superox ...... operties in vitro and in vivo.
@en
P2093
Diane E Cabelli
Donald M Kurtz
Joseph P Emerson
P2860
P304
P356
10.1073/PNAS.0537177100
P407
P577
2003-03-13T00:00:00Z