A Second Nitrogenase-like Enzyme for Bacteriochlorophyll Biosynthesis

@article{Nomata2006ASN,
  title={A Second Nitrogenase-like Enzyme for Bacteriochlorophyll Biosynthesis},
  author={Jiro Nomata and T. Mizoguchi and H. Tamiaki and Y. Fujita},
  journal={Journal of Biological Chemistry},
  year={2006},
  volume={281},
  pages={15021 - 15028}
}
In most photosynthetic organisms, the chlorin ring structure of chlorophyll a is formed by the reduction of the porphyrin D-ring by the dark-operative nitrogenase-like enzyme, protochlorophyllide reductase (DPOR). Subsequently, the chlorin B-ring is reduced in bacteriochlorophyll biosynthesis to form a bacteriochlorin ring structure. Phenotypic analysis of mutants lacking one of three genes, bchX, bchY, or bchZ, which show significant sequence similarity to the structural genes of nitrogenase… Expand
Biochemical Analysis of Two Catalytic Components of Nitrogenase-Like Enzymes Protochlorophyllide Reductase and Chlorophyllide a Reductase from Rhodobacter capsulatus
Bacteriochlorophyll a has a bacteriochlorin ring structure that is formed from a porphyrin ring by the sequential actions of two nitrogenase-like enzymes the dark-operative protochlorophyllideExpand
Reconstitution of a sequential reaction of two nitrogenase-like enzymes in the bacteriochlorophyll biosynthetic pathway of Rhodobacter capsulatus.
TLDR
This reconstitution system confirmed the recent finding that COR catalyzes 8-vinyl reduction of 8.vinyl chlorophyllide a in addition to the known activity of C7C8 double bond reduction, and provides a promising model to investigate how two nitrogenase-like enzymes are coordinated in bacteriochlorophyll biosynthesis. Expand
Chimeric Nitrogenase-like Enzymes of (Bacterio)chlorophyll Biosynthesis*
TLDR
A site-directed mutagenesis approach yielded 10 DPOR mutants for the characterization of amino acid residues involved in protein-protein interaction, indicating a conserved docking surface for the interaction of both DPOR protein subunits. Expand
An unexpectedly branched biosynthetic pathway for bacteriochlorophyll b capable of absorbing near-infrared light
TLDR
The present data indicate that the plasticity of the nitrogenase-like enzyme caused the branched pathways of BChls a and b biosynthesis, ultimately leading to ecologically different niches of B Chl a- and b-based photosynthesis differentiated by more than 150 nm wavelength. Expand
Enzymatic Systems with Homology to Nitrogenase: Biosynthesis of Bacteriochlorophyll and Coenzyme F430.
TLDR
This chapter will focus on the recent progress toward the understanding of the nitrogenase-like enzymes COR and CfbC/D, with special emphasis on the underlying enzymatic mechanism(s). Expand
Engineered biosynthesis of bacteriochlorophyll b in Rhodobacter sphaeroides
TLDR
It has been demonstrated that the enzyme from bacteriochlorophyll a-utilizing bacteria can catalyze the formation of compounds carrying an ethyl group at C8 from both ethyl- and vinyl- carrying substrates, indicating a surprising additional C8-vinyl reductase function. Expand
Chlorophyllide a Oxidoreductase Works as One of the Divinyl Reductases Specifically Involved in Bacteriochlorophyll a Biosynthesis*
TLDR
A double mutant lacking BciA and COR of the purple bacterium Rhodobacter sphaeroides is made to investigate whether the mutant still produces pigments with the C8 ethyl group or if COR actually works as the third DVR, which is suggested to be the evolutionarily oldest DVR among three DVRs. Expand
Expression, Purification, and Activity Analysis of Chlorophyllide Oxidoreductase and Ni2+-Sirohydrochlorin a,c-Diamide Reductase.
TLDR
This chapter describes the production and purification of the COR components, the measurement of COR activity, and the trapping of the ternary COR complex and the strategy for obtaining homogenous and catalytically active preparations of CfbC2 and CfbD2 and a suitable method for extracting the reaction product Ni2+-hexahydrosirohydrochlorin a,c-diamide. Expand
Functional expression of nitrogenase-like protochlorophyllide reductase from Rhodobacter capsulatus in Escherichia coli.
  • Haruki Yamamoto, Jiro Nomata, Yuichi Fuita
  • Biology, Medicine
  • Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology
  • 2008
TLDR
These E. coli strains provide a promising system for structural and kinetic analyses of the nitrogenase-like enzymes, and two overexpression plasmids for L-protein and NB-protein were constructed. Expand
Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase with MgADP bound: a homologue of the nitrogenase Fe protein.
TLDR
The newly determined structure of BchL and its comparison to its close homologue, the nitrogenase Fe protein, provide the basis for understanding how these highly related proteins can discriminate between their respective functions in microbial systems where each must function simultaneously. Expand
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TLDR
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