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Titolo:
Quaternary structure of rice nonsymbiotic hemoglobin
Autore:
Goodman, MD; Hargrove, MS;
Indirizzi:
Iowa State Univ, Dept Biochem Biophys & Mol Biol, Ames, IA 50011 USA Iowa State Univ Ames IA USA 50011 Biophys & Mol Biol, Ames, IA 50011 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 9, volume: 276, anno: 2001,
pagine: 6834 - 6839
SICI:
0021-9258(20010302)276:9<6834:QSORNH>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEME-BASED SENSORS; ESCHERICHIA-COLI; PROTEIN; GENE; KINETICS; BINDING; PLANT; LEGHEMOGLOBIN; PARASPONIA; LIGANDS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Hargrove, MS Iowa State Univ, Dept Biochem Biophys & Mol Biol, Ames, IA 50011 USA Iowa State Univ Ames IA USA 50011 l Biol, Ames, IA 50011 USA
Citazione:
M.D. Goodman e M.S. Hargrove, "Quaternary structure of rice nonsymbiotic hemoglobin", J BIOL CHEM, 276(9), 2001, pp. 6834-6839

Abstract

Plant nonsymbiotic hemoglobins are hexacoordinate heme proteins found in all plants. Although expression is linked with hypoxic environmental conditions (Taylor, E. R., Nie, X. Z., Alexander, W. M., and Hill, R. D. (1994) Plant Mel. Biol. 24, 853-862), no discrete physio logical function has yet been attributed to this family of proteins. The crystal structure of a nonsymbiotic hemo globin from rice has recently been determined. The crystalline protein is homodimeric and hexacoordinate with two histidine side chains coordinating the heme iron atom. Despite the fact that the amino acids responsible for the subunit interface are relatively conserved among the nonsymbiotic hemoglobins, previous work suggests that this group of proteins might display variability in quaternary structure (Duff, S. M. G., Wittenberg, J. B., and Hill, R. D. (1997) J. Biol. Chem. 272, 16746-16752; Arredondo-Peter, R., Hargrove, M. S., Sarath, G., Moran, J. F., Lohrman, J., Olson, J. S., and Klucas, R. V. (1997) Plant Physiol. 115, 1259-1266). Analytical ultracentrifugation and size exclusion high pressure liquid chromatography were used to investigate the quaternary structure of rice nonsymbiotic hemoglobin at various states of ligation and oxidation. Additionally, site-directed mutagenesis was used to test the role of several interface amino acids in dimer formation and ligand binding. Results were analyzed in light of possible physiological functions and indicate that the plant nonsymbiotic hemoglobins are not oxygen transport proteins but more closely resemble known oxygen sensors.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 07:57:38