Nicotinamide is a specific inhibitor of dark-operative protochlorophyllide oxidoreductase, a nitrogenase-like enzyme, from Rhodobacter capsulatus
- PMID: 23954297
- DOI: 10.1016/j.febslet.2013.07.054
Nicotinamide is a specific inhibitor of dark-operative protochlorophyllide oxidoreductase, a nitrogenase-like enzyme, from Rhodobacter capsulatus
Abstract
Dark-operative protochlorophyllide oxidoreductase (DPOR) is a nitrogenase-like enzyme consisting of two components, L-protein as a reductase component and NB-protein as a catalytic component. Elucidation of the crystal structures of NB-protein (Muraki et al., Nature 2010, 465: 110-114) has enabled us to study its reaction mechanism in combination with biochemical analysis. Here we demonstrate that nicotinamide (NA) inhibits DPOR activity by blocking the electron transfer from L-protein to NB-protein. A reaction scheme of DPOR, in which the binding of protochlorophyllide (Pchlide) to the NB-protein precedes the electron transfer from the L-protein, is proposed based on the NA effects.
Keywords: Bacteriochlorophyll; Bchl; Chl; Chlide; Chlorophyll; DPOR; FeS cluster; LPOR; NA; Nitrogenase; Pchlide; Protochlorophyllide; bacteriochlorophyll; chlorophyll; chlorophyllide a; dark-operative protochlorophyllide oxidoreductase; light-dependent protochlorophyllide oxidoreductase; nicotinamide; protochlorophyllide.
Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Similar articles
-
Stoichiometry of ATP hydrolysis and chlorophyllide formation of dark-operative protochlorophyllide oxidoreductase from Rhodobacter capsulatus.Biochem Biophys Res Commun. 2016 Feb 12;470(3):704-709. doi: 10.1016/j.bbrc.2016.01.070. Epub 2016 Jan 13. Biochem Biophys Res Commun. 2016. PMID: 26774340
-
Functional expression of nitrogenase-like protochlorophyllide reductase from Rhodobacter capsulatus in Escherichia coli.Photochem Photobiol Sci. 2008 Oct;7(10):1238-42. doi: 10.1039/b802427h. Epub 2008 Jul 1. Photochem Photobiol Sci. 2008. PMID: 18846289
-
Reconstitution of a sequential reaction of two nitrogenase-like enzymes in the bacteriochlorophyll biosynthetic pathway of Rhodobacter capsulatus.Biochem Biophys Res Commun. 2014 May 30;448(2):200-5. doi: 10.1016/j.bbrc.2014.04.087. Epub 2014 Apr 24. Biochem Biophys Res Commun. 2014. PMID: 24769479
-
Reduction of Chemically Stable Multibonds: Nitrogenase-Like Biosynthesis of Tetrapyrroles.Adv Exp Med Biol. 2017;925:147-161. doi: 10.1007/5584_2016_175. Adv Exp Med Biol. 2017. PMID: 27957709 Review.
-
Evolution of light-independent protochlorophyllide oxidoreductase.Protoplasma. 2019 Mar;256(2):293-312. doi: 10.1007/s00709-018-1317-y. Epub 2018 Oct 6. Protoplasma. 2019. PMID: 30291443 Review.
Cited by
-
The flexible N-terminus of BchL autoinhibits activity through interaction with its [4Fe-4S] cluster and released upon ATP binding.J Biol Chem. 2021 Jan-Jun;296:100107. doi: 10.1074/jbc.RA120.016278. Epub 2020 Dec 3. J Biol Chem. 2021. PMID: 33219127 Free PMC article.
-
Dark-operative protochlorophyllide oxidoreductase generates substrate radicals by an iron-sulphur cluster in bacteriochlorophyll biosynthesis.Sci Rep. 2014 Jun 26;4:5455. doi: 10.1038/srep05455. Sci Rep. 2014. PMID: 24965831 Free PMC article.
-
Substrate recognition induces sequential electron transfer across subunits in the nitrogenase-like DPOR complex.J Biol Chem. 2020 Sep 25;295(39):13630-13639. doi: 10.1074/jbc.RA120.015151. Epub 2020 Jul 31. J Biol Chem. 2020. PMID: 32737200 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Miscellaneous