Nitrate reduction byDesulfovibrio desulfuricans: A periplasmic nitrate reductase system that lacks NapB, but includes a unique tetrahemec-type cytochrome, NapM
Open Access
- 1 July 2005
- journal article
- Published by Oxford University Press (OUP) in FEMS Microbiology Letters
- Vol. 248 (2) , 217-225
- https://doi.org/10.1016/j.femsle.2005.05.042
Abstract
Many sulphate reducing bacteria can also reduce nitrite, but relatively few isolates are known to reduce nitrate. Although nitrate reductase genes are absent from Desulfovibrio vulgaris strain Hildenborough, for which the complete genome sequence has been reported, a single subunit periplasmic nitrate reductase, NapA, was purified from Desulfovibrio desulfuricans strain 27774, and the structural gene was cloned and sequenced. Chromosome walking methods have now been used to determine the complete sequence of the nap gene cluster from this organism. The data confirm the absence of a napB homologue, but reveal a novel six-gene organisation, napC-napM–napA–napD–napG–napH. The NapC polypeptide is more similar to the NrfH subgroup of tetraheme cytochromes than to NapC from other bacteria. NapM is predicted to be a tetra-heme c-type cytochrome with similarity to the small tetraheme cytochromes from Shewanella oneidensis. The operon is located close to a gene encoding a lysyl-tRNA synthetase that is also found in D. vulgaris. We suggest that electrons might be transferred to NapA either from menaquinol via NapC, or from other electron donors such as formate or hydrogen via the small tetraheme cytochrome, NapM. We also suggest that, despite the absence of a twin-arginine targeting sequence, NapG might be located in the periplasm where it would provide an alternative direct electron donor to NapA.Keywords
This publication has 19 references indexed in Scilit:
- NapGH components of the periplasmic nitrate reductase of Escherichia coli K-12: location, topology and physiological roles in quinol oxidation and redox balancingBiochemical Journal, 2004
- The Tetraheme Cytochrome CymA Is Required for Anaerobic Respiration with Dimethyl Sulfoxide and Nitrite inShewanella oneidensisBiochemistry, 2003
- Identification of two domains and distal histidine ligands to the four haems in the bacterial c-type cytochrome NapC; the prototype connector between quinol/quinone and periplasmic oxido-reductasesBiochemical Journal, 2002
- Crystal Structures at Atomic Resolution Reveal the Novel Concept of “Electron-harvesting” as a Role for the Small Tetraheme Cytochrome cJournal of Biological Chemistry, 2002
- Universal Fast Walking for direct and versatile determination of flanking sequenceGene, 2002
- Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanionsPublished by Elsevier ,1999
- Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methodsStructure, 1999
- Cloning and sequence of cymA, a gene encoding a tetraheme cytochrome c required for reduction of iron(III), fumarate, and nitrate by Shewanella putrefaciens MR-1Journal of Bacteriology, 1997
- Isolation and preliminary characterization of a soluble nitrate reductase from the sulfate reducing organism Desulfovibrio desulfuricans ATCC 27774Anaerobe, 1995
- Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotrophaEuropean Journal of Biochemistry, 1994