Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A

@article{Bertero2003InsightsIT,
  title={Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A},
  author={Michela G Bertero and Richard A. Rothery and Monica Palak and Cynthia Hou and Daniel Lim and Francis Blasco and Joel H. Weiner and Natalie C. J. Strynadka},
  journal={Nature Structural Biology},
  year={2003},
  volume={10},
  pages={681-687}
}
The facultative anaerobe Escherichia coli is able to assemble specific respiratory chains by synthesis of appropriate dehydrogenases and reductases in response to the availability of specific substrates. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (nitrate reductase A; NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. We present here the crystal… 
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The present article focuses on the advances obtained on NarGHI, its function and architecture, and the eight redox cofactors that form like an electrical wire through all the enzymes, starting from the electron acceptor site to the catalytic center.
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The crystal structure of QFR from the anaerobic sulphate-reducing bacterium Desulfovibrio gigas is reported and electron/proton-transfer pathways in the quinol reduction of fumarate to succinate in the D. gigas QFR are proposed.
A new paradigm for electron transfer through Escherichia coli nitrate reductase A.
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It is proposed that the role of such anticooperative redox behavior in vivo is to facilitate transmembrane electron transfer across an energy-conserving membrane against an electrochemical potential.
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An overview on the current advances in structural and functional aspects of bacterial nitrate reductases is presented, focusing on the mechanistic implications drawn from the crystallographic data.
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It is established that NarJ ensures complete maturation of the b-type cytochrome subunit NarI by a proper timing for membrane anchoring of the NarGH complex by orchestrating both the maturation and the assembly steps.
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The di-heme family of respiratory complex II enzymes.
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The sulfur shift: an activation mechanism for periplasmic nitrate reductase and formate dehydrogenase.
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The results indicated that the sulfur-shift mechanism provides an efficient way to enable the metal ion for substrate coordination.
S- and N-Oxide Reductases.
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This chapter discusses the complex regulation of the dmsABC and torCAD operons, the poorly understood paralogues, and what is known about the assembly and translocation to the periplasmic space by the Tat translocon.
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