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Microbiology 143 (1997), 3633-3647
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microbiology, Vol 143, 3633-3647, Copyright © 1997 by Society for General Microbiology


ARTICLES

A 12-cistron Escherichia coli operon (hyf) encoding a putative proton- translocating formate hydrogenlyase system

SC Andrews, BC Berks, J McClay, A Ambler, MA Quail, P Golby and JR Guest
Krebs Institute, Department of Molecular Biology & Biotechnology, University of Sheffield, UK. s.andrews@sheffield.ac.uk

The nucleotide sequence has been determined for a twelve-gene operon of Escherichia coli designated the hyf operon (hyfABCDEFGHIR-focB). The hyf operon is located at 55.8-56.0 min and encodes a putative nine- subunit hydrogenase complex (hydrogenase four or Hyf), a potential formate- and sigma 54-dependent transcriptional activator, HyfR (related to FhlA), and a possible formate transporter, FocB (related to FocA). Five of the nine Hyf-complex subunits are related to subunits of both the E. coli hydrogenase-3 complex (Hyc) and the proton- translocating NADH:quinone oxidoreductases (complex I and Nuo), whereas two Hyf subunits are related solely to NADH:quinone oxidoreductase subunits. The Hyf components include a predicted 523 residue [Ni-Fe] hydrogenase (large subunit) with an N-terminus (residues 1-170) homologous to the 30 kDa or NuoC subunit of complex I. It is proposed that Hyf, in conjunction with formate dehydrogenase H (Fdh-H), forms a hitherto unrecognized respiration-linked proton-translocating formate hydrogenlyase (FHL-2). It is likely that HyfR acts as a formate- dependent regulator of the hyf operon and that FocB provides the Hyf complex with external formate as substrate.


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