title: Reduction of Chemically Stable Multibonds: Nitrogenase-Like Biosynthesis of Tetrapyrroles.
abstract: The sophisticated biochemistry of nitrogenase plays a fundamental role for the biosynthesis of tetrapyrrole molecules, acting as key components of photosynthesis and methanogenesis. Three nitrogenase-like metalloenzymes have been characterized to date. Synthesis of chlorophylls and bacteriochlorophylls involves the reduction of the C17-C18 double bond of the conjugated ring system of protochlorophyllide which is catalyzed by the multi-subunit enzyme dark operative protochlorophyllide oxidoreductase (DPOR). Subsequently, biosynthesis of all bacteriochlorophylls requires the reduction of the C7-C8 double bond by a second nitrogenase-like enzyme termed chlorophyllide oxidoreductase (COR). Mechanistically, DPOR and COR make use of a reductase component which links ATP hydrolysis to conformational changes. This dynamic switch protein is triggering the transient association between the reductase and the core catalytic protein complex, thereby facilitating the transduction of electrons via two [4Fe4S] clusters. X-ray crystallographic structural investigations in combination with biochemical experiments revealed the molecular basis of the underlying energy transduction mechanism. The unique nickel-containing tetrapyrrole cofactor F430is located in the active site of methyl-coenzyme M reductase, which is catalyzing the final step of methane formation in methanogenic archaea. The nitrogenase-like protein NflH/NflD has been proposed to catalyze one or more ring reduction steps during the biosynthesis of F430. The present working hypothesis mirrors a DPOR and COR related enzyme mechanism of NflH/NflD. Furthermore, nfl-encoded proteins were suggested as "simplified" ancestors lying basal in the phylogenetic tree between nitrogenase and DPOR/COR.
authors.affiliation: Institut für Biochemie, Universität Leipzig, Brüderstraße 34, D-04103, Leipzig, Germany.
authors.forename: Gunhild
authors.initials: G
authors.lastname: Layer
authors.affiliation: Institut für Pflanzenbiologie, Technische Universität Braunschweig, Spielmannstraße 7, D-38106, Braunschweig, Germany.
authors.forename: Joern
authors.initials: J
authors.lastname: Krausze
authors.affiliation: Institut für Mikrobiologie, Technische Universität Braunschweig, Spielmannstraße 7, D-38106, Braunschweig, Germany. j.moser@tu-bs.de.
authors.forename: Jürgen
authors.initials: J
authors.lastname: Moser
mesh_terms: D016948:Azotobacter vinelandii / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001429:Bacteriochlorophylls / Q000096:biosynthesis / Q000737:chemistry*; D055162:Biocatalysis; D015870:Gene Expression; D009591:Nitrogenase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D044925:Oxidoreductases Acting on CH-CH Group Donors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010788:Photosynthesis / Q000235:genetics; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D054730:Protein Interaction Domains and Motifs; D017434:Protein Structure, Tertiary; D016354:Rhodobacter capsulatus / Q000235:genetics / Q000378:metabolism; D041904:Roseobacter / Q000235:genetics / Q000378:metabolism; D045725:Tetrapyrroles / Q000096:biosynthesis / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D001429:Bacteriochlorophylls; D045725:Tetrapyrroles; D010088:Oxidoreductases; D009591:Nitrogenase; D044925:Oxidoreductases Acting on CH-CH Group Donors; C511363:chlorophyllide a reductase, Rhodobacter capsulatus; C023886:protochlorophyllide reductase; C021572:methyl coenzyme M reductase
keywords: Chlorophyll biosynthesis; Chlorophyllide oxidoreductase; Cofactor F430 biosynthesis; Dark operative protochlorophyllide oxidoreductase; Nitrogenase-like enzyme