Carbonyl sulfide hydrolase from thiobacillus thioparus strain thi115 is one of the β-carbonic anhydrase family enzymes

Takahiro Ogawa, Keiichi Noguchi, Masahiko Saito, Yoshiko Nagahata, Hiromi Kato, Akashi Ohtaki, Hiroshi Nakayama, Naoshi Dohmae, Yasuhiko Matsushita, Masafumi Odaka, Masafumi Yohda, Hiroshi Nyunoya, Yoko Katayama

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

Carbonyl sulfide (COS) is an atmospheric trace gas leading to sulfate aerosol formation, thereby participating in the global radiation balance and ozone chemistry, but its biological sinks are not well understood. Thiobacillus thioparus strain THI115 can grow on thiocyanate (SCN-) as its sole energy source. Previously, we showed that SCN- is first converted to COS by thiocyanate hydrolase in T. thioparus strain THI115. In the present work, we purified, characterized, and determined the crystal structure of carbonyl sulfide hydrolase (COSase), which is responsible for the degradation of COS to H2S and CO2, the second step of SCN- assimilation. COSase is a homotetramer composed of a 23.4 kDa subunit containing a zinc ion in its catalytic site. The amino acid sequence of COSase is homologous to the β-class carbonic anhydrases (β-CAs). Although the crystal structure including the catalytic site resembles those of the β-CAs, CO2 hydration activity of COSase is negligible compared to those of the β-CAs. The α5 helix and the extra loop (Gly150-Pro158) near the N-terminus of the α6 helix narrow the substrate pathway, which could be responsible for the substrate specificity. The k cat/Km value, 9.6 × 105 s-1 M-1, is comparable to those of the β-CAs. COSase hydrolyzes COS over a wide concentration range, including the ambient level, in vitro and in vivo. COSase and its structurally related enzymes are distributed in the clade D in the phylogenetic tree of β-CAs, suggesting that COSase and its related enzymes are one of the catalysts responsible for the global sink of COS.

Original languageEnglish
Pages (from-to)3818-3825
Number of pages8
JournalJournal of the American Chemical Society
Volume135
Issue number10
DOIs
Publication statusPublished - 2013 Mar 13
Externally publishedYes

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Carbonic anhydrase
Thiobacillus
Hydrolases
Carbonic Anhydrases
Enzymes
carbonyl sulfide
Sulfides
Catalytic Domain
Crystal structure
Ozone
Substrates
Substrate Specificity
Aerosols
Hydration
Sulfates

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Carbonyl sulfide hydrolase from thiobacillus thioparus strain thi115 is one of the β-carbonic anhydrase family enzymes. / Ogawa, Takahiro; Noguchi, Keiichi; Saito, Masahiko; Nagahata, Yoshiko; Kato, Hiromi; Ohtaki, Akashi; Nakayama, Hiroshi; Dohmae, Naoshi; Matsushita, Yasuhiko; Odaka, Masafumi; Yohda, Masafumi; Nyunoya, Hiroshi; Katayama, Yoko.

In: Journal of the American Chemical Society, Vol. 135, No. 10, 13.03.2013, p. 3818-3825.

Research output: Contribution to journalArticle

Ogawa, T, Noguchi, K, Saito, M, Nagahata, Y, Kato, H, Ohtaki, A, Nakayama, H, Dohmae, N, Matsushita, Y, Odaka, M, Yohda, M, Nyunoya, H & Katayama, Y 2013, 'Carbonyl sulfide hydrolase from thiobacillus thioparus strain thi115 is one of the β-carbonic anhydrase family enzymes', Journal of the American Chemical Society, vol. 135, no. 10, pp. 3818-3825. https://doi.org/10.1021/ja307735e
Ogawa, Takahiro ; Noguchi, Keiichi ; Saito, Masahiko ; Nagahata, Yoshiko ; Kato, Hiromi ; Ohtaki, Akashi ; Nakayama, Hiroshi ; Dohmae, Naoshi ; Matsushita, Yasuhiko ; Odaka, Masafumi ; Yohda, Masafumi ; Nyunoya, Hiroshi ; Katayama, Yoko. / Carbonyl sulfide hydrolase from thiobacillus thioparus strain thi115 is one of the β-carbonic anhydrase family enzymes. In: Journal of the American Chemical Society. 2013 ; Vol. 135, No. 10. pp. 3818-3825.
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AU - Ogawa, Takahiro

AU - Noguchi, Keiichi

AU - Saito, Masahiko

AU - Nagahata, Yoshiko

AU - Kato, Hiromi

AU - Ohtaki, Akashi

AU - Nakayama, Hiroshi

AU - Dohmae, Naoshi

AU - Matsushita, Yasuhiko

AU - Odaka, Masafumi

AU - Yohda, Masafumi

AU - Nyunoya, Hiroshi

AU - Katayama, Yoko

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N2 - Carbonyl sulfide (COS) is an atmospheric trace gas leading to sulfate aerosol formation, thereby participating in the global radiation balance and ozone chemistry, but its biological sinks are not well understood. Thiobacillus thioparus strain THI115 can grow on thiocyanate (SCN-) as its sole energy source. Previously, we showed that SCN- is first converted to COS by thiocyanate hydrolase in T. thioparus strain THI115. In the present work, we purified, characterized, and determined the crystal structure of carbonyl sulfide hydrolase (COSase), which is responsible for the degradation of COS to H2S and CO2, the second step of SCN- assimilation. COSase is a homotetramer composed of a 23.4 kDa subunit containing a zinc ion in its catalytic site. The amino acid sequence of COSase is homologous to the β-class carbonic anhydrases (β-CAs). Although the crystal structure including the catalytic site resembles those of the β-CAs, CO2 hydration activity of COSase is negligible compared to those of the β-CAs. The α5 helix and the extra loop (Gly150-Pro158) near the N-terminus of the α6 helix narrow the substrate pathway, which could be responsible for the substrate specificity. The k cat/Km value, 9.6 × 105 s-1 M-1, is comparable to those of the β-CAs. COSase hydrolyzes COS over a wide concentration range, including the ambient level, in vitro and in vivo. COSase and its structurally related enzymes are distributed in the clade D in the phylogenetic tree of β-CAs, suggesting that COSase and its related enzymes are one of the catalysts responsible for the global sink of COS.

AB - Carbonyl sulfide (COS) is an atmospheric trace gas leading to sulfate aerosol formation, thereby participating in the global radiation balance and ozone chemistry, but its biological sinks are not well understood. Thiobacillus thioparus strain THI115 can grow on thiocyanate (SCN-) as its sole energy source. Previously, we showed that SCN- is first converted to COS by thiocyanate hydrolase in T. thioparus strain THI115. In the present work, we purified, characterized, and determined the crystal structure of carbonyl sulfide hydrolase (COSase), which is responsible for the degradation of COS to H2S and CO2, the second step of SCN- assimilation. COSase is a homotetramer composed of a 23.4 kDa subunit containing a zinc ion in its catalytic site. The amino acid sequence of COSase is homologous to the β-class carbonic anhydrases (β-CAs). Although the crystal structure including the catalytic site resembles those of the β-CAs, CO2 hydration activity of COSase is negligible compared to those of the β-CAs. The α5 helix and the extra loop (Gly150-Pro158) near the N-terminus of the α6 helix narrow the substrate pathway, which could be responsible for the substrate specificity. The k cat/Km value, 9.6 × 105 s-1 M-1, is comparable to those of the β-CAs. COSase hydrolyzes COS over a wide concentration range, including the ambient level, in vitro and in vivo. COSase and its structurally related enzymes are distributed in the clade D in the phylogenetic tree of β-CAs, suggesting that COSase and its related enzymes are one of the catalysts responsible for the global sink of COS.

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