Expression, Purification, Physicochemical Characterization and Structural Analysis of Cytochromec554fromVibrio parahaemolyticusStrain RIMD2210633

Akazaki, Hideharu; Kawai, Fumihiro; Chida, Hirotaka; Hirano, Tetsufumi; Hakamata, Wataru; Park, Sam-Yong; Nishio, Takeshi; Oku, Tatsuo

doi:10.1271/bbb.90943

Cited by 3 publications

(2 citation statements)

References 9 publications

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“…MCA1068, MCA2603, and MCA0940 show sequence similarities to cytochrome c 554 from Vibrio parahaemolyticus and cytochrome c 4 from Pseudomonas stutzeri (Kadziola and Larsen ; Akazaki et al. ). MCA0940 differs from other class I cytochromes c by having an extended region between the CxxCH motif and the methionine forming the sixth heme‐coordinating ligand.…”

Section: Resultsmentioning

confidence: 99%

Transcriptomic profiling ofMethylococcus capsulatus(Bath) during growth with two different methane monooxygenases

Larsen

Karlsen

2015

MicrobiologyOpen

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Methylococcus capsulatus (Bath) is a methanotroph that possesses both a membrane‐embedded (pMMO) and a soluble methane monooxygenase (sMMO). The expression of these two MMO's is tightly controlled by the availability of copper in the growth medium, but the underlying mechanisms and the number of genes involved in this switch in methane oxidation is not yet fully elucidated. Microarray analyses were used to assess the transcriptome in cells producing either pMMO or sMMO. A total of 137 genes were differentially expressed, with 87 genes showing a significant up‐regulation during sMMO production. The majority of the differentially expressed genes could be assigned to functional roles in the energy metabolism and transport. Furthermore, three copper responding gene clusters were discovered, including an extended cluster that also harbors the genes for sMMO. Our data also indicates that major changes takes place in the respiratory chain between pMMO‐ and sMMO‐producing cells, and that quinone are predominantly used as the electron donors for methane oxidation by pMMO. Intriguingly, a large proportion of the differentially expressed genes between pMMO‐ and sMMO‐producing cells encode c‐type cytochromes. By combining microarray‐ and mass spectrometry data, a total of 35 c‐type cytochromes are apparently expressed in M. capsulatus when grown in nitrate mineral salt medium with methane as sole energy and carbon source, and the expression of 21 of these respond to the availability of copper. Interestingly, several of these c‐type cytochromes are recovered from the cell surface, suggesting that extracellular electron transfers may occur in M. capsulatus.

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Section: Resultsmentioning

confidence: 99%

Transcriptomic profiling ofMethylococcus capsulatus(Bath) during growth with two different methane monooxygenases

Larsen

Karlsen

2015

MicrobiologyOpen

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“…Crystal structures of proteins in Group I have interfaces between the two monomers closely mimicking the interdomain interface in c 4 , through a two-fold axis centered at the middle of the hydrogen bond between the two inner HPs of the hemes (Figure S16A). For homodimers in Group I, the calculated SASA values of the heme group are 40–60 Å 2 and reduction potentials of the heme iron are 250–280 mV. − The SASA values of c 4 -A and c 4 -B domains in the intact full-length c 4 (Table S4) are similar. When, however, the second monoheme molecule for each structure in Group I is removed during analysis, the SASA values increase to 100–140 Å 2 , similar to what happens in c 4 -A and c 4 -B in the absence of the other domain.…”

Section: Discussionmentioning

confidence: 99%

Influence of the Interdomain Interface on Structural and Redox Properties of Multiheme Proteins

et al. 2022

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Multiheme proteins are important in energy conversion and biogeochemical cycles of nitrogen and sulfur. A diheme cytochrome c 4 (c 4) was used as a model to elucidate roles of the interdomain interface on properties of iron centers in its hemes A and B. Isolated monoheme domains c 4-A and c 4-B, together with the full-length diheme c 4 and its Met-to-His ligand variants, were characterized by a variety of spectroscopic and stability measurements. In both isolated domains, the heme iron is Met/His-ligated at pH 5.0, as in the full-length c 4, but becomes His/His-ligated in c 4-B at higher pH. Intradomain contacts in c 4-A are minimally affected by the separation of c 4-A and c 4-B domains, and isolated c 4-A is folded. In contrast, the isolated c 4-B is partially unfolded, and the interface with c 4-A guides folding of this domain. The c 4-A and c 4-B domains have the propensity to interact even without the polypeptide linker. Thermodynamic cycles have revealed properties of monomeric folded isolated domains, suggesting that ferrous (FeII), but not ferric (FeIII) c 4-A and c 4-B, is stabilized by the interface. This study illustrates the effects of the interface on tuning structural and redox properties of multiheme proteins and enriches our understanding of redox-dependent complexation.

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Comparative proteomic profiling reveals specific adaption of Vibrio anguillarum to oxidative stress, iron deprivation and humoral components of innate immunity

Skåne

Loose

Vaaje‐Kolstad

et al. 2022

Journal of Proteomics

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Expression, Purification, Physicochemical Characterization and Structural Analysis of Cytochromec₅₅₄fromVibrio parahaemolyticusStrain RIMD2210633

Cited by 3 publications

References 9 publications

Transcriptomic profiling ofMethylococcus capsulatus(Bath) during growth with two different methane monooxygenases

Transcriptomic profiling ofMethylococcus capsulatus(Bath) during growth with two different methane monooxygenases

Influence of the Interdomain Interface on Structural and Redox Properties of Multiheme Proteins

Comparative proteomic profiling reveals specific adaption of Vibrio anguillarum to oxidative stress, iron deprivation and humoral components of innate immunity

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