Title

The Periplasmic Nitrate Reductase of Thiosphaera pantotropha

Document Type

Article

Language

eng

Format of Original

10 p.

Publication Date

8-1995

Publisher

Elsevier

Source Publication

Journal of Inorganic Biochemistry

Source ISSN

0162-0134

Original Item ID

doi: 10.1111/j.1432-1033.1994.00789.x

Abstract

The aerobically-active periplasmic respiratory nitrate reductase (Nap) from the bacterium Thiosphaera pantotropha is a heterodimer of NapA (90kDa), which binds molybdopterin guanine dinucleotide (MGD) and a [4Fe-4S] cluster (Em,7 = -160mV), and NapB (16kDa) which contains two, probably bis - His co-ordinated, c-type haem groups (Em,7 = -15mV and +80mV) [1-4]. Mov EPR has detected sets of signals typical of molybdenum-dependent hydroxylases as well as signals typical of molybdenum-containing reductases [3]. The two sets of signals are proposed to reflect differences in the cofactor pterin oxidation state. Oxidation by nitrate in the presence of cyanide of enzyme displaying hydroxylase-like signals generates a very unusual Mov signal with gav >2.0. Magnetic interactions between Mo and the [Fe-S] cluster were not observed. The napEDABC locus coding for the periplasmic nitrate reductase system has been cloned and sequenced [4]. Sequence comparisons with other MGD-dependent enzymes allows proposal of a region of NapA involved in formation of the active site. Mov EPR and active site sequence comparisons indicate that the Mo environment in Nap is similar to that in bacterial assimilatory nitrate reductase but distinct from that in bacterial membrane-bound respiratory nitrate reductases and support the presence of a cysteine Mo ligand, napC appears to code for a membrane-anchored tetrahaem cytochrome c of the NirT family. NapC is likely to be the direct physiological electron donor to NapAB and may also be a ubiquinol oxidase.

Comments

Journal of Inorganic Biochemistry, Vol. 59, No. 2-3 (August 1995): 728. DOI.

Brian Bennett was affiliated with the University of East Anglia at the time of publication.