TY - JOUR
T1 - Preference for particular lanthanide species and thermal stability of XoxFs in Methylorubrum extorquens strain AM1
AU - Wang, Lun
AU - Hibino, Ayumi
AU - Suganuma, Souya
AU - Ebihara, Akio
AU - Iwamoto, Satoshi
AU - Mitsui, Ryoji
AU - Tani, Akio
AU - Shimada, Masaya
AU - Hayakawa, Takashi
AU - Nakagawa, Tomoyuki
N1 - Funding Information:
This research was funded in part by a Grant-in-Aid for Scientific Research (B) No. 17H03949 (to TN), and was also supported by the Joint Usage/Research Center , Institute of Plant Science and Resources , Okayama University, Japan .
Publisher Copyright:
© 2020 Elsevier Inc.
PY - 2020/5
Y1 - 2020/5
N2 - XoxF-type methanol dehydrogenase was recently found to be lanthanide-dependent, while its counterpart MxaF is Ca2+-dependent. The lanthanide (Ln) series consists of 15 different elements, all of which exist in nature, although at different relative abundances. XoxF from Methylorubrum extorquens strain AM1 has been shown to be induced by four light Ln species (La3+ to Nd3+). The preference of XoxFs for certain co-existing Ln species and the catalytic activity and stability of XoxF metallated with different Ln species have not been well investigated. In this study, we found that (i) strain AM1 cells preferentially utilize La3+ rather than Nd3+ for growth, (ii) XoxF purified from cells grown with a La3+ and Nd3+ mixture contained a larger proportion of La3+, and (iii) La3+-metallated XoxF has higher activity and thermal stability than Nd3+-metallated XoxF, although (iv) both enzymes showed unchanged surface charges. Thermal shift assay in particular revealed that metallation affects the temperature for subunit denaturation but not for subunit dissociation. We concluded that, although La3+ and Nd3+ have similar distributions in nature, XoxF could chose La3+ preferentially, likely because of its higher Lewis acidity, which is important for the catalytic activity of the enzyme.
AB - XoxF-type methanol dehydrogenase was recently found to be lanthanide-dependent, while its counterpart MxaF is Ca2+-dependent. The lanthanide (Ln) series consists of 15 different elements, all of which exist in nature, although at different relative abundances. XoxF from Methylorubrum extorquens strain AM1 has been shown to be induced by four light Ln species (La3+ to Nd3+). The preference of XoxFs for certain co-existing Ln species and the catalytic activity and stability of XoxF metallated with different Ln species have not been well investigated. In this study, we found that (i) strain AM1 cells preferentially utilize La3+ rather than Nd3+ for growth, (ii) XoxF purified from cells grown with a La3+ and Nd3+ mixture contained a larger proportion of La3+, and (iii) La3+-metallated XoxF has higher activity and thermal stability than Nd3+-metallated XoxF, although (iv) both enzymes showed unchanged surface charges. Thermal shift assay in particular revealed that metallation affects the temperature for subunit denaturation but not for subunit dissociation. We concluded that, although La3+ and Nd3+ have similar distributions in nature, XoxF could chose La3+ preferentially, likely because of its higher Lewis acidity, which is important for the catalytic activity of the enzyme.
KW - Lanthanide
KW - Methanol dehydrogenase
KW - Methylotrophs
KW - XoxF1
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U2 - 10.1016/j.enzmictec.2020.109518
DO - 10.1016/j.enzmictec.2020.109518
M3 - Article
C2 - 32331722
AN - SCOPUS:85078779476
VL - 136
JO - Enzyme and Microbial Technology
JF - Enzyme and Microbial Technology
SN - 0141-0229
M1 - 109518
ER -