Over-expression of membrane-bound cytochrome c-551 from thermophilic Bacillus PS3 in Bacillus stearothermophilus K1041

Noguchi, Shunsuke; Yamazaki, T.; Yaginuma, Atsuo; Sakamoto, Junshi; Sone, Nobuhito

doi:10.1016/0005-2728(94)90049-3

Cited by 15 publications

(6 citation statements)

References 27 publications

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“…The cytochrome c-550 gene consisted of 357 bp with a Shine-Dalgano (SD) sequence (AGGAGG) preceding the gene 7 bp upstream of a methionine-coding start codon. The cytochrome c appeared to consist of 118 amino acids, including a putative 17-residue signal peptide sequence referred to in previous reports(Noguchi et al 1994;Albert et al 1998; Sutcliffe and Harrington 2002). The cytochrome c-550 polypeptide contained one heme c binding motif (CXXCH).…”

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confidence: 66%

A novel membrane-anchored cytochrome c-550 of alkaliphilic Bacillus clarkii K24-1U: expression, molecular features and properties of redox potential

et al. 2009

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A membrane-anchored cytochrome c-550, which is highly expressed in obligately alkaliphilic Bacillus clarkii K24-1U, was purified and characterized. The protein contained a conspicuous sequence of Gly(22)-Asn(34), in comparison with the other Bacillus small cytochromes c. Analytical data indicated that the original and lipase-treated intermediate forms of cytochrome c-550 bind to fatty acids of C(15), C(16) and C(17) chain lengths and C(15) chain length, respectively, and it was considered that these fatty acids are bound to glycerol-Cys(18). Since there was a possibility that the presence of a diacylglycerol anchor contributed to the formation of dimeric states of this protein (20 and 17 kDa in SDS-PAGE), a C18M (Cys(18) --> Met)-cytochrome c-550 was constructed. The molecular mass of the C18M-cytochrome c-550 was determined as 15 and 10 kDa in SDS-PAGE and 23 kDa in blue native PAGE. The C18M-cytochrome c-550 bound with or without Triton X-100 formed a tetramer as the original cytochrome c-550 bound with Triton X-100, as determined by gel filtration. The midpoint redox potential of cytochrome c-550 as determined by redox titration was +83 mV, while that determined by cyclic voltammetric measurement was +7 mV. The above results indicate that cytochrome c-550 is a novel cytochrome c.

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confidence: 66%

A novel membrane-anchored cytochrome c-550 of alkaliphilic Bacillus clarkii K24-1U: expression, molecular features and properties of redox potential

et al. 2009

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“…Undigested cytochrome c 551 migrates as a single peak. Two additional peaks with shorter elution times were obtained after incubation with lipase for 3 and 7 h. These two peaks likely represent cytochrome c 511 having lost one and two lipoyl moieties, respectively ( , ). Unfortunately, because of proteolytic activity in the lipase preparation, incubation could not be performed for periods longer than 7 h, preventing complete conversion (data not shown).…”

Section: Resultsmentioning

confidence: 99%

“…Small c cytochromes are anchored to the membrane via a transmembrane α-helix or by (close to) N-terminal covalently bound lipids ( − ). Cytochrome c 511 is anchored to the membrane via a covalently bound lipid.…”

Section: Resultsmentioning

confidence: 99%

“…When purified cytochrome c 551 was incubated with lipase, its mobility on butyl-Sepharose increased, yielding two new peaks indicating the presence of a covalently bound lipid consisting of two lipoyl moieties. The covalent attachment of lipids to protein N-terminal cysteine residues is an important general mechanism for anchoring small c-type cytochromes to the cytoplasmic membrane of Gram-positive bacteria (23) and also in Gram-negative bacteria such as the photosynthetic reaction center in Rhodopseudomonas Viridis (26).…”

Section: Discussionmentioning

confidence: 99%

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NO Reductase from Bacillus azotoformans Is a Bifunctional Enzyme Accepting Electrons from Menaquinol and a Specific Endogenous Membrane-Bound Cytochrome c₅₅₁

2004

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Bacillus azotoformans is a Gram-positive denitrifying soil bacterium, which is capable of respiring nitrate, nitrite, nitric oxide, and nitrous oxide under anaerobic conditions. It contains a unique menaquinol-dependent nitric oxide reductase (qCu(A)NOR) with a Cu(A) center in its small subunit. The qCu(A)NOR exhibits menaquinol-dependent NO reductase activity, whereas reduced horse heart cytochrome c was inactive. Here we describe the purification of three membrane-bound c cytochromes from B. azotoformans. Their apparent molecular masses on SDS-PAGE are approximately 11 kDa. At neutral pH, these c cytochromes are negatively charged and the E(m) for all is close to 150 mV. Only one of these c cytochromes, which exhibits an alpha-band maximum at 551 nm, acts as a direct electron donor to qCu(A)NOR. Further investigation demonstrated that this cytochrome c(551) possesses two lipoyl moieties, which presumably function to anchor it to the membrane. Steady-state kinetic studies reveal that cytochrome c(551) is a noncompetitive inhibitor of NO reduction when menaquinol is used as an electron donor. This finding points to the presence of two different electron donation pathways in qCu(A)NOR. The ability of qCu(A)NOR to accept electrons from both menaquinol and cytochrome c(551) might be related to the regulation of the rate of NO reduction especially as a defense mechanism of B. azotoformans against the toxicity of NO. Growth experiments in batch culture indeed show that B. azotoformans is highly NO tolerant, in contrast to, for example, Paracoccus denitrificans that has a monofunctional cytochrome c-dependent NOR. We propose that the menaquinol pathway, which has a 4-fold greater maximal activity than the pathway via cytochrome c(551), is used for NO detoxification, whereas electron donation via the endogenous cytochrome c involves the cytochrome b(6)f complex serving the bioenergetic needs of the organism.

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“…The presence of a lipase in a Hase maturation operon is unprecedented and prompted us to examine the effect of a lipase on the [NiFeSe] m Hase. For this we used a Rhyzopus lipase as previously described [11]. The reaction mixture containing the [NiFeSe] m Hase and lipase was analysed by HPLC at different time points.…”

Section: Resultsmentioning

confidence: 99%

The [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough is a bacterial lipoprotein lacking a typical lipoprotein signal peptide

et al. 2007

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Desulfovibrio vulgaris Hildenborough has a membrane-bound [NiFeSe] hydrogenase whose mode of membrane association was unknown since it is constituted by two hydrophilic subunits. This work shows that this hydrogenase is a bacterial lipoprotein bound to the membrane by lipidic groups found at the N-terminus of the large subunit, which is unusual since it is missing the typical lipoprotein signal peptide. Nevertheless, the large subunit has a conserved four residue lipobox and its synthesis is sensitive to the signal peptidase II inhibitor globomycin. The D. vulgaris [NiFeSe] hydrogenase is the first example of a bacterial lipoprotein translocated through the Tat pathway.

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Over-expression of membrane-bound cytochrome c-551 from thermophilic Bacillus PS3 in Bacillus stearothermophilus K1041

Cited by 15 publications

References 27 publications

A novel membrane-anchored cytochrome c-550 of alkaliphilic Bacillus clarkii K24-1U: expression, molecular features and properties of redox potential

A novel membrane-anchored cytochrome c-550 of alkaliphilic Bacillus clarkii K24-1U: expression, molecular features and properties of redox potential

NO Reductase from Bacillus azotoformans Is a Bifunctional Enzyme Accepting Electrons from Menaquinol and a Specific Endogenous Membrane-Bound Cytochrome c₅₅₁

The [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough is a bacterial lipoprotein lacking a typical lipoprotein signal peptide

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Over-expression of membrane-bound cytochrome c-551 from thermophilic Bacillus PS3 in Bacillus stearothermophilus K1041

Cited by 15 publications

References 27 publications

A novel membrane-anchored cytochrome c-550 of alkaliphilic Bacillus clarkii K24-1U: expression, molecular features and properties of redox potential

A novel membrane-anchored cytochrome c-550 of alkaliphilic Bacillus clarkii K24-1U: expression, molecular features and properties of redox potential

NO Reductase from Bacillus azotoformans Is a Bifunctional Enzyme Accepting Electrons from Menaquinol and a Specific Endogenous Membrane-Bound Cytochrome c551

The [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough is a bacterial lipoprotein lacking a typical lipoprotein signal peptide

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NO Reductase from Bacillus azotoformans Is a Bifunctional Enzyme Accepting Electrons from Menaquinol and a Specific Endogenous Membrane-Bound Cytochrome c₅₅₁