The haem b558 component of the cytochrome bd quinol oxidase complex from Escherichia coli has histidine-methionine axial ligation

Spinner, Frank; Cheesman, Myles R.; Thomson, Andrew J.; Kaysser, Tamma M.; Gennis, Robert; Peng, Qinyun; Peterson, Jim

doi:10.1042/bj3080641

Cited by 48 publications

(42 citation statements)

References 35 publications

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“…A69611). Three of the four axial ligands to the irons of the three hemes have been identified as His-19, His-186, and Met-393 of CydA (subunit I) in the E. coli cytochrome bd oxidase (25,40,68,69). The corresponding residues are conserved as His-18, His-183, and Met-333 in M. thermoacetica CydA.…”

Section: Resultsmentioning

confidence: 99%

Cytochrome bd Oxidase, Oxidative Stress, and Dioxygen Tolerance of the Strictly Anaerobic Bacterium Moorella thermoacetica

Das¹,

Silaghi-Dumitrescu

Ljungdahl³

et al. 2005

J Bacteriol

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The gram-positive, thermophilic, acetogenic bacterium Moorella thermoacetica can reduce CO 2 to acetate via the Wood-Ljungdahl (acetyl coenzyme A synthesis) pathway. This report demonstrates that, despite its classification as a strict anaerobe, M. thermoacetica contains a membrane-bound cytochrome bd oxidase that can catalyze reduction of low levels of dioxygen. Whole-cell suspensions of M. thermoacetica had significant endogenous O 2 uptake activity, and this activity was increased in the presence of methanol or CO, which are substrates in the Wood-Ljungdahl pathway. Cyanide and azide strongly (ϳ70%) inhibited both the endogenous and CO/methanol-dependent O 2 uptake. UV-visible light absorption and electron paramagnetic resonance spectra of n-dodecyl-␤-maltoside extracts of M. thermoacetica membranes showed the presence of a cytochrome bd oxidase complex containing cytochrome b 561 , cytochrome b 595 , and cytochrome d (chlorin). Subunits I and II of the bd oxidase were identified by N-terminal amino acid sequencing. The M. thermoacetica cytochrome bd oxidase exhibited cyanide-sensitive quinol oxidase activity. The M. thermoacetica cytochrome bd (cyd) operon consists of four genes, encoding subunits I and II along with two ABC-type transporter proteins, homologs of which in other bacteria are required for assembly of the bd complex. The level of this cyd operon transcript was significantly increased when M. thermoacetica was grown in the absence of added reducing agent (cysteine ؉ H 2 S). Expression of a 35-kDa cytosolic protein, identified as a cysteine synthase (CysK), was also induced by the nonreducing growth conditions. The combined evidence indicates that cytochrome bd oxidase and cysteine synthase protect against oxidative stress and contribute to the limited dioxygen tolerance of M. thermoacetica.Dioxygen is the preferred electron sink in the respiratory chain of most aerobic bacteria (58). Cytochrome oxidases are the membrane-bound, terminal components of the dioxygendependent respiratory chain, which reduces dioxygen to water with formation of pH and potential gradients (6, 45). Two main types of respiratory cytochrome oxidases are known in bacteria: the heme/copper oxidases (cytochrome aa 3 , cytochrome caa 3 oxidase, and cytochrome bo oxidase), and the heme-only cytochrome bd quinol oxidase, which is associated with microaerobic dioxygen respiration (24,56,59,62). Cytochrome bd oxidases purified from aerobic bacteria have been characterized as 1:1 heterodimers of two integral membrane proteins referred to as subunits I and II (35,55). The heterodimers contain three heme components: a low-spin heme, b 558 , and two high-spin hemes, b 595 and d. In the genomes of Escherichia coli (31) and Azotobacter vinelandii (41), subunits I and II are encoded by cydA and cydB, respectively, of the cytochrome bd (cyd) operon. Two ABC-type transporter proteins, CydD and CydC, are typically required for assembly of the cytochrome bd complex in both gram-positive and gram-negative aerobic bacteria (14, 60). Aerobic r...

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Section: Resultsmentioning

confidence: 99%

Cytochrome bd Oxidase, Oxidative Stress, and Dioxygen Tolerance of the Strictly Anaerobic Bacterium Moorella thermoacetica

Das¹,

Silaghi-Dumitrescu

Ljungdahl³

et al. 2005

J Bacteriol

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“…The small isolated peak at g ϭ 3.47 is the g z feature of the second limiting type of low-spin ferric heme EPR, a "large g max " spectrum for which the g y and g x features are broad and often not detected (42). Again, these features are not unique to any one pair of axial ligands, and there are a number of examples in the literature of such spectra arising from both His/His and His/Met coordination (43)(44)(45).…”

Section: Fig 2 Multiple Sequence Alignments Of Ccoo and Ccopmentioning

confidence: 99%

Molecular and Spectroscopic Analysis of the Cytochromecbb3 Oxidase from Pseudomonas stutzeri

Pitcher¹,

Cheesman²,

Watmough³

2002

Journal of Biological Chemistry

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Cytochrome cbb 3 oxidase, a member of the heme-copper oxidase superfamily, is characterized by its high affinity for oxygen while retaining the ability to pump protons. These attributes are central to its proposed role in the microaerobic metabolism of proteobacteria. We have completed the first detailed spectroscopic characterization of a cytochrome cbb 3 oxidase, the enzyme purified from Pseudomonas stutzeri. A combination of UVvisible and magnetic CD spectroscopies clearly identified four low-spin hemes and the high-spin heme of the active site. This heme complement is in good agreement with our analysis of the primary sequence of the ccoNOPQ operon and biochemical analysis of the complex. Near-IR magnetic CD spectroscopy revealed the unexpected presence of a low-spin bishistidine-coordinated c-type heme in the complex. This was shown to be one of two c-type hemes in the CcoP subunit by separately expressing the subunit in Escherichia coli. Separate expression of CcoP also allowed us to unambiguously assign each of the signals associated with low-spin ferric hemes present in the X-band EPR spectrum of the oxidized enzyme. This work both underpins future mechanistic studies on this distinctive class of bacterial oxidases and raises questions concerning the role of CcoP in electron delivery to the catalytic subunit.

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“…The horizontal bar indicates the periplasmic Q-loop of CydA, which contains the proposed quinol-binding site, and the corresponding shorter region in CioA. of spectroscopic methods Fang et al, 1989;Jiang et al, 1993;Spinner et al, 1995). These studies have identified His-186 and Met-393 of CydA as the ligands to haem b 558 .…”

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

124

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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The haem b558 component of the cytochrome bd quinol oxidase complex from Escherichia coli has histidine-methionine axial ligation

Cited by 48 publications

References 35 publications

Cytochrome bd Oxidase, Oxidative Stress, and Dioxygen Tolerance of the Strictly Anaerobic Bacterium Moorella thermoacetica

Cytochrome bd Oxidase, Oxidative Stress, and Dioxygen Tolerance of the Strictly Anaerobic Bacterium Moorella thermoacetica

Molecular and Spectroscopic Analysis of the Cytochromecbb3 Oxidase from Pseudomonas stutzeri

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

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