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FEBS Letters
Article . 2006 . Peer-reviewed
License: Wiley Online Library User Agreement
Data sources: Crossref
FEBS Letters
Article . 2007
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Nitrogenase Fe protein‐like Fe–S cluster is conserved in L‐protein (BchL) of dark‐operative protochlorophyllide reductase from Rhodobacter capsulatus

Authors: Nomata, Jiro; Kitashima, Masaharu; Inoue, Kazuhito; Fujita, Yuichi;

Nitrogenase Fe protein‐like Fe–S cluster is conserved in L‐protein (BchL) of dark‐operative protochlorophyllide reductase from Rhodobacter capsulatus

Abstract

Dark‐operative protochlorophyllide reductase (DPOR) in bacteriochlorophyll biosynthesis is a nitrogenase‐like enzyme consisting of L‐protein (BchL‐dimer) as a reductase component and NB‐protein (BchN–BchB‐heterotetramer) as a catalytic component. Metallocenters of DPOR have not been identified. Here we report that L‐protein has an oxygen‐sensitive [4Fe–4S] cluster similar to nitrogenase Fe protein. Purified L‐protein from Rhodobacter capsulatus showed absorption spectra and an electron paramagnetic resonance signal indicative of a [4Fe–4S] cluster. The activity quickly disappeared upon exposure to air with a half‐life of 20 s. These results suggest that the electron transfer mechanism is conserved in nitrogenase Fe protein and DPOR L‐protein.

Keywords

Iron-Sulfur Proteins, Oxidoreductases Acting on CH-CH Group Donors, Spectrum Analysis, Electron Spin Resonance Spectroscopy, Light-Harvesting Protein Complexes, Bacteriochlorophyll biosynthesis, Fe–S cluster, Rhodobacter capsulatus, Bacterial Proteins, Nitrogenase, Oxidoreductases, Protochlorophyllide reductase, Conserved Sequence, BchL

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
58
Top 10%
Top 10%
Top 10%