Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase
Autore:
Kurisu, G; Kusunoki, M; Katoh, E; Yamazaki, T; Teshima, K; Onda, Y; Kimata-Ariga, Y; Hase, T;
Indirizzi:
Osaka Univ, Inst Prot Res, Res Ctr Struct Biol, Suita, Osaka 5650871, Japan Osaka Univ Suita Osaka Japan 5650871 ct Biol, Suita, Osaka 5650871, Japan Natl Inst Agrobiol Resources, Dept Biotechnol, Tsukuba, Ibaraki 3058602, Japan Natl Inst Agrobiol Resources Tsukuba Ibaraki Japan 3058602 3058602, Japan Hiroshima Univ, Fac Integrated Arts & Sci, Higashihiroshima, Hiroshima 7398521, Japan Hiroshima Univ Higashihiroshima Hiroshima Japan 7398521 ma 7398521, Japan Osaka Univ, Inst Prot Res, Div Enzymol, Suita, Osaka 5650871, Japan Osaka Univ Suita Osaka Japan 5650871 Enzymol, Suita, Osaka 5650871, Japan
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 2, volume: 8, anno: 2001,
pagine: 117 - 121
SICI:
1072-8368(200102)8:2<117:SOTETC>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHTHALATE DIOXYGENASE REDUCTASE; 1.7 ANGSTROM RESOLUTION; NADP+ REDUCTASE; ANABAENA FERREDOXIN; DEPENDENT ENZYMES; 2FE-2S FERREDOXIN; BINDING-SITES; SPINACH; SURFACE; CRYSTALLOGRAPHY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Kurisu, G Osaka Univ, Inst Prot Res, Res Ctr Struct Biol, 2-2 Yamadaoka, Suita, Osaka 5650871, Japan Osaka Univ 2-2 Yamadaoka Suita Osaka Japan 5650871 650871, Japan
Citazione:
G. Kurisu et al., "Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase", NAT ST BIOL, 8(2), 2001, pp. 117-121

Abstract

All oxygenic photosynthetically derived reducing equivalents are utilized by combinations of a single multifuctional electron carrier protein, ferredoxin (Fd), and several Fd-dependent oxidoreductases, We report the first crystal structure of the complex between maize leaf Pd and Fd-NADP(+) oxidoreductase (FNR), The redox centers in the complex - the 2Fe-2S cluster of Pd and flavin adenine dinucleotide (FAD) of FNR - are in close proximity; the shortest distance is 6.0 Angstrom. The intermolecular interactions in the complex are mainly electrostatic, occurring through salt bridges, and the interface near the prosthetic groups is hydrophobic. NMR experiments on the complex in solution confirmed the FNR recognition sites on Fd that are identified in the crystal structure. interestingly. the structures of Pd and FNRin the complex and in the free state differ in several ways. For example, in the active site of FNR, Pd binding induces the formation of a new hydrogen bond between side chains of Glu 312 and Ser 96 of FNR. We propose that this type of molecular communication not only determines the optimal orientation of the two proteins for electron transfer, but also contributes to themodulation of the enzymatic properties of FNR.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/01/20 alle ore 12:25:42