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

  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},
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… 
The Membrane‐Bound Nitrate Reductase A from Escherichia Coli: NarGHI
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.
Structural insights into the electron/proton transfer pathways in the quinol:fumarate reductase from Desulfovibrio gigas
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.
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.
Structural and mechanistic insights on nitrate reductases
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.
Biogenesis of a Respiratory Complex Is Orchestrated by a Single Accessory Protein*
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.
Biosynthesis of the respiratory formate dehydrogenases from Escherichia coli: characterization of the FdhE protein
It is shown that E. coli FdhE interacts with the catalytic subunits of the respiratory formate dehydrogenases, and site-directed mutagenesis shows that conserved cysteine motifs are essential for the physiological activity of the Fdh E protein and are also involved in iron ligation.
The di-heme family of respiratory complex II enzymes.
  • C. Lancaster
  • Chemistry, Biology
    Biochimica et biophysica acta
  • 2013
The sulfur shift: an activation mechanism for periplasmic nitrate reductase and formate dehydrogenase.
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.
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.


The coordination and function of the redox centres of the membrane-bound nitrate reductases
A global architecture for the Mo-bisMGD-containing subunit (NarG) and a coordination model for the four [Fe–S] centres of the electron-transfer sub unit (NarH) and for the two b-type haems of the anchor subunit NarI are discussed.
Molecular Basis of Proton Motive Force Generation: Structure of Formate Dehydrogenase-N
The structure of the membrane protein formate dehydrogenase-N (Fdn-N), a major component of Escherichia coli nitrate respiration, has been determined and provides critical insights into the proton motive force generation by redox loop, a common mechanism among a wide range of respiratory enzymes.
The diheme cytochrome b subunit (Narl) of Escherichia coli nitrate reductase A (NarGHI): structure, function, and interaction with quinols.
This minireview focuses on recent advances and future prospects for the diheme cytochrome b subunit (Narl) of NarGHI, a complex iron-sulfur molybdoenzyme of Escherichia coli.
Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution
The crystal structure of the three protein subunits containing fumarate reductase from the anaerobic bacterium Wolinella succinogenes is described and a pathway of electron transfer from the dihaem cytochrome b to the site offumarate reduction and a mechanism of fUMarate reduction is proposed.
Sites and specificity of the reaction of bipyridylium compounds with anaerobic respiratory enzymes of Escherichia coli. Effects of permeability barriers imposed by the cytoplasmic membrane.
The ability of the oxidized and singly reduced species of several bipyridylium cations to cross the cytoplasmic membrane of Escherichia coli was studied to locate the sites of reaction of the dyes
Architecture of Succinate Dehydrogenase and Reactive Oxygen Species Generation
The structure of Escherichia colisuccinate dehydrogenase (SQR), analogous to the mitochondrial respiratory complex II, has been determined, revealing the electron transport pathway from the electron
Sequence analysis of subunits of the membrane‐bound nitrate reductase from a denitrifying bacterium: the integral membrane subunit provides a prototype for the dihaem electron‐carrying arm of a redox loop
Two pairs of conserved histidine residues in the integral membrane subunits of these enzymes that are appropriately positioned to bind one haem towards each side of the membrane bilayer are identified.
Crystal Structure of Formate Dehydrogenase H: Catalysis Involving Mo, Molybdopterin, Selenocysteine, and an Fe4S4 Cluster
Crystal structures of the oxidized and reduced formate dehydrogenase H form have been determined, revealing a four-domain αβ structure with the molybdenum directly coordinated to selenium and both MGD cofactors, which suggest a reaction mechanism that directly involves SeCys140 and His141 in proton abstraction and the Molybdopterin, Lys44, and the Fe4S4 cluster in electron transfer.
Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 A resolution.
The periplasmic trimethylamine N-oxide (TMAO) reductase from the marine bacteria Shewanella massilia is involved in a respiratory chain, having trimethylamine N-oxide as terminal electron acceptor.