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Titolo:
Redox properties and coordination structure of the heme in the CO-sensing transcriptional activator CooA
Autore:
Nakajima, H; Honma, Y; Tawara, T; Kato, T; Park, SY; Miyatake, H; Shiro, Y; Aono, S;
Indirizzi:
Japan Adv Inst Sci & Technol, Sch Mat Sci, Tatsunokuchi, Ishikawa 9231292,Japan Japan Adv Inst Sci & Technol Tatsunokuchi Ishikawa Japan 9231292 92,Japan RIKEN, Harima Inst, Mikazuki, Hyogo 6795148, Japan RIKEN Mikazuki Hyogo Japan 6795148 a Inst, Mikazuki, Hyogo 6795148, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 10, volume: 276, anno: 2001,
pagine: 7055 - 7061
SICI:
0021-9258(20010309)276:10<7055:RPACSO>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
SOLUBLE GUANYLATE-CYCLASE; LIGAND BOND LENGTHS; OXYGEN SENSOR FIXL; SCATTERING XAFS ANALYSES; RESONANCE RAMAN-SPECTROSCOPY; RHODOSPIRILLUM-RUBRUM; NITRIC-OXIDE; RHIZOBIUM-MELILOTI; CARBON-MONOXIDE; ABSORPTION SPECTROSCOPIES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Aono, S Japan Adv Inst Sci & Technol, Sch Mat Sci, 1-1 Asahidai, Tatsunokuchi, Ishikawa 9231292, Japan Japan Adv Inst Sci & Technol 1-1 Asahidai Tatsunokuchi Ishikawa Japan 9231292
Citazione:
H. Nakajima et al., "Redox properties and coordination structure of the heme in the CO-sensing transcriptional activator CooA", J BIOL CHEM, 276(10), 2001, pp. 7055-7061

Abstract

The CO-sensing transcriptional activator CooA contains a six-coordinate protoheme as a CO sensor. Cys(75) and His(77) are assigned to the fifth ligand of the ferric and ferrous hemes, respectively. In this study, we carried out alanine-scanning mutagenesis and EXAFS analyses to determine the coordination structure of the heme in CooA. Pro(2) is thought to be the sixth ligand of the ferric and ferrous hemes in CooA, which is consistent with the crystal structure of ferrous CooA (Lanzilotta, W, N., Schuller, D. J., Thorsteinsson, M. V., Kerby, R, L,, Roberts, G. P., and Poulos, T. L. (2000) Not. Struct Biol. 7, 876-880). CooA exhibited anomalous redox chemistry, i.e. hysteresis was observed in electrochemical redox titrations in which the observed reduction and oxidation midpoint potentials were -320 mV and -260 mV, respectively. The redox-controlled ligand exchange of the heme between Cys(75) and His(77) is thought to cause the difference between the reduction and oxidation midpoint potentials.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 02:09:30