A missing link between complex I and group 4 membrane-bound [NiFe] hydrogenases.

Complex I of respiratory chains is an energy transducing enzyme present in most bacteria, mitochondria and chloroplasts. It catalyzes the oxidation of NADH and the reduction of quinones, coupled to cation translocation across the membrane. The complex has a modular structure composed of several proteins most of which are identified in other complexes. Close relations between complex I and group 4 membrane-bound [NiFe] hydrogenases and some subunits of multiple resistance to pH (Mrp) Na(+)/H(+) antiporters have been observed before and the suggestion that complex I arose from the association of a soluble nicotinamide adenine dinucleotide (NAD(+)) reducing hydrogenase with a Mrp-like antiporter has been put forward. In this article we performed a thorough taxonomic profile of prokaryotic group 4 membrane-bound [NiFe] hydrogenases, complexes I and complex I-like enzymes. In addition we have investigated the different gene clustering organizations of such complexes. Our data show the presence of complexes related to hydrogenases but which do not contain the binding site of the catalytic centre. These complexes, named before as Ehr (energy-converting hydrogenases related complexes) are a missing link between complex I and group 4 membrane-bound [NiFe] hydrogenases. Based on our observations we put forward a different perspective for the relation between complex I and related complexes. In addition we discuss the evolutionary, functional and mechanistic implications of this new perspective. This article is part of a Special Issue entitled: The evolutionary aspects of bioenergetic systems.