Resonance raman study on axial ligands of heme irons in cytochrome bd‐type ubiquinol oxidase from Escherichia coli

Hirota, Shun; Mogi, Tatsushi; Anraku, Yasuhiro; Gennis, Robert B.; Kitagawa, Teizo

doi:10.1002/bspy.350010502

Cited by 20 publications

(17 citation statements)

References 33 publications

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“…A number of other amino acids have been proposed as potential ligands to haem d, including tyrosine residues as is the case in some catalases, methionine as in c-type cytochromes, and cysteine which is found in cytochrome P450, chloroperoxidase and NO synthases. C214 in CydB has been suggested as a potential haem ligand but it is not conserved in CioB (Hirota et al, 1995). Two of the four histidines present in E. coli CydB are conserved in A. vinelandii CydB but not in CioB or AppB (Fig.…”

Section: Figmentioning

confidence: 99%

“…1B). The consensus of recent spectral data from electron paramagnetic resonance (EPR), electron nuclear double resonance (ENDOR), Fouriertransform infra-red spectroscopy (FT-IR) and resonance Raman studies of cytochrome bd is that the proximal ligand is not cysteine or methionine, and that if it is a histidine or strong nitrogenous ligand then the residue is in an unusual environment (Tsubaki et al, 1993;Hirota et al, 1995).…”

Section: Figmentioning

confidence: 99%

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The cioAB genes from Pseudomonas aeruginosa code for a novel cyanide‐insensitive terminal oxidase related to the cytochrome bd quinol oxidases

Cunningham

Pitt

Williams

1997

Molecular Microbiology

126

156

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SummaryThe structural genes for the cyanide-insensitive terminal oxidase (CIO) of Pseudomonas aeruginosa were sequenced. The locus comprised two open reading frames, cioA and cioB, coding for gene products of 488 and 335 amino acid residues with predicted molecular masses of 54 241 and 37 016 Da respectively. These genes were encoded by a 2.7 kb transcript and probably comprise an operon. Upstream of a major transcriptional start site is a ¹10 promoter region and, approximately at nucleotides ¹50 and þ13, there are sequences homologous to the binding site of the transcriptional regulator Anr. The deduced amino acid sequences of CioA and CioB are homologous to the cytochrome bd quinol oxidases of Escherichia coli and Azotobacter vinelandii. However, no cytochrome d -like signals were found in wild-type P. aeruginosa strains. An atypical cytochrome d -like signal was seen under low-aeration growth conditions but only in strains in which the cioAB genes were present on a high-copy-number plasmid. The appearance of these cytochrome d -like signals was not paralleled by a concomitant increase in CIO activity. These data support the hypothesis that the CIO of P. aeruginosa does not contain haem d. This raises the possibility that there is a family of bacterial quinol oxidases related to the cytochrome bd of E. coli that can differ in their haem composition from the E. coli paradigm.

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Section: Figmentioning

confidence: 99%

Section: Figmentioning

confidence: 99%

The cioAB genes from Pseudomonas aeruginosa code for a novel cyanide‐insensitive terminal oxidase related to the cytochrome bd quinol oxidases

Cunningham

Pitt

Williams

1997

Molecular Microbiology

126

156

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“…Purification of Cytochrome bd and Quinol Oxidase Assay-The enzyme was isolated from the cytochrome bd-overproducing strain GR84N/pNG2 (34), as described previously (14). The concentration of the enzyme was calculated from the Soret absorption of the air-oxidized form by using an extinction coefficient of 223,000 M Ϫ1 cm Ϫ1 (35).…”

Section: Methodsmentioning

confidence: 99%

Mass Spectrometric Analysis of the Ubiquinol-binding Site in Cytochrome bd from Escherichia coli

Matsumoto

Murai

Fujita

et al. 2006

Journal of Biological Chemistry

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Cytochrome bd is a heterodimeric terminal ubiquinol oxidase in the aerobic respiratory chain of Escherichia coli. For understanding the unique catalytic mechanism of the quinol oxidation, mass spectrometry was used to identify amino acid residue(s) that can be labeled with a reduced form of 2-azido-3-methoxy-5-methyl-6-geranyl-1,4-benzoquinone or 2-methoxy-3-azido-5-methyl-6-geranyl-1,4-benzoquinone. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry demonstrated that the photo inactivation of ubiquinol-1 oxidase activity was accompanied by the labeling of subunit I with both azidoquinols. The cross- Cytochrome bd (CydAB) is a heterodimeric ubiquinol oxidase in the aerobic respiratory chain of Escherichia coli and is predominantly expressed under microaerophilic growth conditions (see Refs. 1-3 for reviews). It catalyzes dioxygen reduction with two molecules of ubiquinol-8 (Q 8 H 2 ), 2 leading to the release of four protons from quinols to the periplasm. Through a putative proton channel, four protons used for dioxygen reduction are taken up from the cytoplasm and delivered to the dioxygen reduction site at the periplasmic side of the cytoplasmic membrane (4). During dioxygen reduction, cytochrome bd generates an electrochemical proton gradient (⌬pH and membrane potential) across the membrane through apparent transmembrane movement of four chemical protons (5-7). In contrast to cytochrome bo, an alternative oxidase under highly aerated growth conditions, cytochrome bd has no proton pumping activity and does not belong to the heme-copper terminal oxidase superfamily.On the basis of spectroscopic and ligand binding studies, three distinct redox metal centers have been identified as heme b 558 , heme b 595 , and heme d (see Ref. 8 for a review). Unlike cytochrome bo, cytochrome bd does not contain a tightly bound Q 8 . Heme b 558 is a low spin protoheme IX and is ligated by I-His 186 (helix V) and I-Met 393 (helix VII) of subunit I (CydA) (9). Heme b 595 is a high spin protoheme IX bound to I-His 19 (helix I) of subunit I (9) and mediates electron transfer from heme b 558 to heme d, where dioxygen is reduced to water (10 -13). Heme d is a high spin chlorin bound to an unidentified nitrogenous ligand (14 -16) and forms a di-heme binuclear center with heme b 595 (16,17). Topological analysis suggests that all of the hemes are located at the periplasmic end of transmembrane helices (4).In loop VI/VII (Q-loop) of subunit I, binding of monoclonal antibodies to 252 KLAAIEAEWET 262 (18,19) and proteolytic cleavage with trypsin at I-Tyr 290 or chymotrypsin at I-Arg 298 (20, 21) suppressed ubiquinol oxidase activity. Photoaffinity labeling studies with 2-methyl-3-azido-5-methoxy-6-(3,7-dimethyl-[ 3 H]octyl)-1,4-benzoquinone ([ 3 H]3-azido-2-methyl-5-methoxy-BQ 2s ) indicate the presence of the quinol oxidation site in subunit I (22). These results suggest that periplasmic loop VI/VII in subunit I is involved in the ubiquinol oxidation site. Inhibitor binding studies indicated the close proximity ...

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“…4 A). A potential heme ligand in EcCydB (C214) [Hirota et al, 1995] is partially conserved ( fig. 4 B).…”

Section: Components Of the Z Mobilis Respiratory Chain Encoded By Itmentioning

confidence: 99%

Analysis of the Respiratory Chain in Ethanologenic Zymomonas mobilis with a Cyanide-Resistant bd-Type Ubiquinol Oxidase as the Only Terminal Oxidase and Its Possible Physiological Roles

et al. 2007

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The respiratory chain of the ethanologenic bacterium Zymomonas mobilis was investigated, in which the pyruvate-to-ethanol pathway has been demonstrated to be mainly responsible for NADH oxidation and the tricarboxylic acid cycle is incomplete. Membranes from cells cultivated under aerobic or anaerobic growth conditions showed dehydrogenase and oxidase activities for NADH, D-lactate and D-glucose and ubiquinol oxidase activity. Intriguingly, the NADH oxidase activity level of membrane fractions from cells grown aerobically was found to be higher than that of membrane fractions from Escherichia coli or Pseudomonas putida grown aerobically, indicating a crucial role of the respiratory chain in NADH oxidation in the organism. Cyanide-resistant terminal oxidase activity was observed and appeared to be due to a bd-type ubiquinol oxidase as the only terminal oxidase encoded by the entire genome. The terminal oxidase with a relatively strong ubiquinol oxidase activity exhibited remarkably weak signals of cytochrome d. Considering these findings and the presence of a type-II NADH dehydrogenase but not a type-I, a simple respiratory chain that generates less energymay have evolved in Z. mobilis.

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Resonance raman study on axial ligands of heme irons in cytochrome bd‐type ubiquinol oxidase from Escherichia coli

Cited by 20 publications

References 33 publications

The cioAB genes from Pseudomonas aeruginosa code for a novel cyanide‐insensitive terminal oxidase related to the cytochrome bd quinol oxidases

The cioAB genes from Pseudomonas aeruginosa code for a novel cyanide‐insensitive terminal oxidase related to the cytochrome bd quinol oxidases

Mass Spectrometric Analysis of the Ubiquinol-binding Site in Cytochrome bd from Escherichia coli

Analysis of the Respiratory Chain in Ethanologenic <i>Zymomonas mobilis</i> with a Cyanide-Resistant <i>bd</i>-Type Ubiquinol Oxidase as the Only Terminal Oxidase and Its Possible Physiological Roles

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