| RRC ID |
34518
|
| 著者 |
Nonaka K, Nguyen NT, Yoon KS, Ogo S.
|
| タイトル |
Novel H2-oxidizing [NiFeSe]hydrogenase from Desulfovibrio vulgaris Miyazaki F.
|
| ジャーナル |
J Biosci Bioeng
|
| Abstract |
[NiFeSe]hydrogenases are promising biocatalysts in H2-based technology due to their high catalytic activity and O2-stability. Here, we report purification and characterization of a new membrane-associated [NiFeSe]hydrogenase from Desulfovibrio vulgaris Miyazaki F ([NiFeSe]DvMF). The [NiFeSe]DvMF was composed of two subunits, corresponding to a large subunit of 58.3 kDa and a small subunit of 29.3 kDa determined by SDS-PAGE. Unlike conventional [NiFeSe]hydrogenases having catalytic bias toward H2-production, the [NiFeSe]DvMF showed 11-fold higher specific activity of H2-oxidation (2444 U/mg) than that of H2-production (217 U/mg). At the optimal reaction temperature of the enzyme (65°C), the specific activity of H2-oxidation could reach up to 21,553 U/mg. Amperometric assays of the [NiFeSe]DvMF clearly indicated that the enzyme had a remarkable O2-stability. According to the amino acid sequence alignment, the conserved cysteine residue at position 281 in medial cluster of other [NiFeSe]hydrogenases was specifically replaced by a serine residue (Ser281) in the [NiFeSe]DvMF. These results indicate that the [NiFeSe]DvMF can play as a new H2-oxidizing and O2-stable biocatalyst, along with providing helpful insights into the structure-function relationship of [NiFeSe]hydrogenases.
|
| 巻・号 |
115(4)
|
| ページ |
366-71
|
| 公開日 |
2013-4-1
|
| DOI |
10.1016/j.jbiosc.2012.10.011
|
| PII |
S1389-1723(12)00437-9
|
| PMID |
23201506
|
| MeSH |
Amino Acid Sequence
Biocatalysis
Desulfovibrio vulgaris / enzymology*
Desulfovibrio vulgaris / genetics
Hydrogenase / chemistry
Hydrogenase / genetics
Hydrogenase / metabolism*
Molecular Sequence Data
Oxidation-Reduction
Sequence Alignment
|
| IF |
2.366
|
| 引用数 |
8
|
|
WOS 分野
|
FOOD SCIENCE & TECHNOLOGY
BIOTECHNOLOGY & APPLIED MICROBIOLOGY
|
| リソース情報 |
| 一般微生物 |
JCM 14930 |
