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Cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774

Cunha, C. A., Macieira, S., Dias, J. M., Almeida, G., Goncalves, L. L., Costa, C., Lampreia, J., Huber, Robert, Moura, J. J. G., Moura, I. and Romao, M. J. 2003. Cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774. Journal of Biological Chemistry 278 (19) , pp. 17455-17465. 10.1074/jbc.M211777200

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Abstract

The gene encoding cytochrome cnitrite reductase (NrfA) from Desulfovibrio desulfuricansATCC 27774 was sequenced and the crystal structure of the enzyme was determined to 2.3-Å resolution. In comparison with homologous structures, it presents structural differences mainly located at the regions surrounding the putative substrate inlet and product outlet, and includes a well defined second calcium site with octahedral geometry, coordinated to propionates of hemes 3 and 4, and caged by a loop non-existent in the previous structures. The highly negative electrostatic potential in the environment around hemes 3 and 4 suggests that the main role of this calcium ion may not be electrostatic but structural, namely in the stabilization of the conformation of the additional loop that cages it and influences the solvent accessibility of heme 4. The NrfA active site is similar to that of peroxidases with a nearby calcium site at the heme distal side nearly in the same location as occurs in the class II and class III peroxidases. This fact suggests that the calcium ion at the distal side of the active site in the NrfA enzymes may have a similar physiological role to that reported for the peroxidases.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Publisher: American Society for Biochemistry and Molecular Biology
ISSN: 0021-9258
Last Modified: 24 Jun 2017 11:00
URI: http://orca-mwe.cf.ac.uk/id/eprint/70191

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