Thermal stability of cytochrome <i>c</i>′ from mesophilic <i>Shewanella amazonensis</i>

Kato, Yuki; Fujii, Sotaro; Kuribayashi, Takaaki; Masanari, Misa; Sambongi, Yoshihiro

doi:10.1080/09168451.2015.1015956

Cited by 7 publications

(2 citation statements)

References 16 publications

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“…Previously, we found that cytochrome c ′ (PHCP) from thermophilic Hydrogenophilus thermoluteolus (formally called Pseudmonas hydrogenothermophila ) growing optimally at 52°C showed high thermal stability compared with cytochrome c ′ (AVCP) from mesophilic Allochromatium vinosum growing optimally at 25–30°C . Cytochrome c ′ from another mesophilic bacterium, Shewanella amazonensis , growing optimally at 37°C exhibited thermal stability that was intermediate between those of AVCP and PHCP . The thermal stability of these three proteins positively correlates with the growth temperatures of the source bacteria, thus a comparative study on protein stability can be carried out using these proteins.…”

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confidence: 99%

Structural and functional insights into thermally stable cytochrome c′ from a thermophile

et al. 2017

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Thermophilic Hydrogenophilus thermoluteolus cytochrome c′ (PHCP) exhibits higher thermal stability than a mesophilic counterpart, Allochromatium vinosum cytochrome c′ (AVCP), which has a homo‐dimeric structure and ligand‐binding ability. To understand the thermal stability mechanism and ligand‐binding ability of the thermally stable PHCP protein, the crystal structure of PHCP was first determined. It formed a homo‐dimeric structure, the main chain root mean square deviation (rmsd) value between PHCP and AVCP being 0.65 Å. In the PHCP structure, six specific residues appeared to strengthen the heme‐related and subunit–subunit interactions, which were not conserved in the AVCP structure. PHCP variants having altered subunit–subunit interactions were more severely destabilized than ones having altered heme‐related interactions. The PHCP structure further revealed a ligand‐binding channel and a penta‐coordinated heme, as observed in the AVCP protein. A spectroscopic study clearly showed that some ligands were bound to the PHCP protein. It is concluded that the dimeric PHCP from the thermophile is effectively stabilized through heme‐related and subunit–subunit interactions with conservation of the ligand‐binding ability.Brief SummaryWe report the X‐ray crystal structure of cytochrome c′ (PHCP) from thermophilic Hydrogenophilus thermoluteolus. The high thermal stability of PHCP was attributed to heme‐related and subunit–subunit interactions, which were confirmed by a mutagenesis study. The ligand‐binding ability of PHCP was examined by spectrophotometry. PHCP acquired the thermal stability with conservation of the ligand‐binding ability. This study furthers the understanding of the stability and function of cytochromes c.

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Section: Introductionmentioning

confidence: 99%

Structural and functional insights into thermally stable cytochrome c′ from a thermophile

et al. 2017

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“…The wide distribution of Shewanella species also makes them suitable bacteria for investigating not only the enzymatic reactions that drive biogeochemical cycles (Falkowski et al 2008), but also the protein stability mechanism as to such various environments. In this context, we have carried out protein thermal stability studies using cytochromes c isolated from a variety of Shewanella species (Ogawa et al 2007;Takenaka et al 2010;Masanari et al 2011;Kato et al 2015). Recently, we found a positive correlation between the optimal growth pressures of four Shewanella species and the stabilities of their highly homologous cytochromes c 5 (Masanari et al 2014;Masanari et al 2016).…”

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Difference in NaCl tolerance of membrane-bound 5′-nucleotidases purified from deep-sea and brackish water Shewanella species

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Shewanella species are widely distributed in sea, brackish, and fresh water areas, growing psychrophilically or mesophilically, and piezophilically or piezo-sensitively. Here, membrane-bound 5'-nucleotidases (NTases) from deep-sea Shewanella violacea and brackish water Shewanella amazonensis were examined from the aspect of NaCl tolerance to gain an insight into protein stability against salt. Both NTases were single polypeptides with molecular masses of ~59 kDa, as determined on mass spectroscopy. They similarly required 10 mM MgCl for their activities, and they exhibited the same pH dependency and substrate specificity for 5'-nucleotides. However, S. violacea 5'-nucleotidase (SVNTase) was active enough in the presence of 2.5 M NaCl, whereas S. amazonensis 5'-nucleotidase (SANTase) exhibited significantly reduced activity with the same concentration of the salt. Although SVNTase and SANTase exhibited high sequence identity (69.7%), differences in the ratio of acidic to basic amino acid residues and the number of potential salt bridges maybe being responsible for the difference in the protein stability against salt. 5'-Nucleotidases from these Shewanella species will provide useful information regarding NaCl tolerance, which may be fundamental for understanding bacterial adaptation to growth environments.

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Extremophilic Enzymes Related to Energy Conversion

Wakai

Sambongi

2018

The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery

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Thermal stability of cytochrome c′ from mesophilic Shewanella amazonensis

Cited by 7 publications

References 16 publications

Structural and functional insights into thermally stable cytochrome c′ from a thermophile

Structural and functional insights into thermally stable cytochrome c′ from a thermophile

Difference in NaCl tolerance of membrane-bound 5′-nucleotidases purified from deep-sea and brackish water Shewanella species

Extremophilic Enzymes Related to Energy Conversion

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