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Titolo:
Iron coordination structures of oxygen sensor FixL characterized by FeK-edge extended x-ray absorption fine structure and resonance Raman spectroscopy
Autore:
Miyatake, H; Mukai, M; Adachi, S; Nakamura, H; Tamura, K; Iizuka, T; Shiro, Y; Strange, RW; Hasnain, SS;
Indirizzi:
RIKEN Harima Inst, Inst Phys & Chem Res, Sayo, Hyogo 6795143, Japan RIKEN Harima Inst Sayo Hyogo Japan 6795143 es, Sayo, Hyogo 6795143, Japan SERC, Daresbury Lab, Warrington WA4 4AD, Cheshire, England SERC Warrington Cheshire England WA4 4AD ngton WA4 4AD, Cheshire, England
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 33, volume: 274, anno: 1999,
pagine: 23176 - 23184
SICI:
0021-9258(19990813)274:33<23176:ICSOOS>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
CURVED-WAVE THEORY; RHIZOBIUM-MELILOTI; KINASE-ACTIVITY; 2-COMPONENT REGULATORS; SIGNAL-TRANSDUCTION; EXAFS CALCULATIONS; LIGAND-BINDING; CO-MYOGLOBINS; HEME PROTEIN; NITRIC-OXIDE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Shiro, Y RIKEN Harima Inst, Inst Phys & Chem Res, Mikazuki Cho, Sayo, Hyogo 6795143, Japan RIKEN Harima Inst Mikazuki Cho Sayo Hyogo Japan 6795143 43, Japan
Citazione:
H. Miyatake et al., "Iron coordination structures of oxygen sensor FixL characterized by FeK-edge extended x-ray absorption fine structure and resonance Raman spectroscopy", J BIOL CHEM, 274(33), 1999, pp. 23176-23184

Abstract

FixL is a heme-based O-2 sensor protein involved in a two-component systemof a symbiotic bacterium, In the present study, the iron coordination structure in the heme domain of Rhizobium meliloti FixLT (RmFixLT, a soluble truncated FixL) was examined using Fe K-edge extended x-ray absorption fine structure (EXAFS) and resonance Raman spectroscopic techniques. In the EXAFSanalyses, the interatomic distances and angles of the Fe-ligand bond and the iron displacement from the heme plane were obtained for RmFixLT in the Fe2+, Fe2+O2, Fe2+CO, Fe3+, Fe3+F-, and Fe3+CN- states. An apparent correlation was found between the heme-nitrogen (proximal His-194) distance in the heme domain and the phosphorylation activity of the histidine kinase domain. Comparison of the Fe-CO coordination geometry between RmFixLT and RmFixLH(heme domain of RmFixL), based on the EXAFS and Raman results, has suggested that the kinase domain directly or indirectly influences steric interaction between the iron-bound ligand and the heme pocket. Referring to the crystal structure of the heme domain of Bradyrhizobium japonicum FixL (Gong, W., Hao, B., Mansy, S. S., Gonzalez, G., Gilles-Gonzalez, M. A., and Chan, M. K. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 15177-15182), we discussed details of the iron coordination structure of RmFixLT and RmFixLH in relation to an intramolecular signal transduction mechanism in its O-2 sensing.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 20:29:11