Role of Amino Acid Residues for Dioxygen Activation in the Second Coordination Sphere of the Dicopper Site of pMMO

Mayuko Miyanishi, Tsukasa Abe, Yuta Hori, Yoshihito Shiota, Kazunari Yoshizawa

Research output: Contribution to journalArticle

Abstract

Formation of an active oxygen species at the dicopper site of pMMO is studied by using density functional theory (DFT) calculations. The role of the amino acid residues of tyrosine (Tyr374) and glutamate (Glu35) located in the second coordination sphere of the dicopper site is discussed in detail. The phenolic proton of the tyrosine residue is transferred to the Cu2O2 core in a two-step manner via the glutamate residue, and an electron is directly transferred to the Cu2O2 core. These proton- and electron-transfer processes induce the O-O bond cleavage of the μ-η2:η2-peroxodicopper(II) species to form the (μ-oxo)(μ-hydroxo)CuIICuIII species, which is able to play a key role of methane hydroxylation at the dicopper site of pMMO ( Inorg. Chem. 2013 , 52 , 7907 ). This proton-coupled electron-transfer mechanism is a little different from that in tyrosinase in that the proton of substrate tyrosine is directly transferred to the dicopper site ( J. Am. Chem. Soc. 2006 , 128 , 9873 ) because there is no proton acceptor in the vicinity of the dicopper site of tyrosinase. The rate-determining step for the formation of the (μ-oxo)(μ-hydroxo)CuIICuIII species is determined to be the O-O bond cleavage. These results shed new light on the interpretation of the role of the tyrosine and glutamate residues located in the second coordination sphere of the dicopper site of pMMO.

Original languageEnglish
Pages (from-to)12280-12288
Number of pages9
JournalInorganic chemistry
Volume58
Issue number18
DOIs
Publication statusPublished - Sep 16 2019

Fingerprint

tyrosine
amino acids
Protons
Chemical activation
glutamates
activation
Tyrosine
Oxygen
Amino Acids
protons
Glutamic Acid
Monophenol Monooxygenase
Electrons
cleavage
electron transfer
Hydroxylation
Methane
Density functional theory
Reactive Oxygen Species
methane

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry

Cite this

Role of Amino Acid Residues for Dioxygen Activation in the Second Coordination Sphere of the Dicopper Site of pMMO. / Miyanishi, Mayuko; Abe, Tsukasa; Hori, Yuta; Shiota, Yoshihito; Yoshizawa, Kazunari.

In: Inorganic chemistry, Vol. 58, No. 18, 16.09.2019, p. 12280-12288.

Research output: Contribution to journalArticle

@article{886d0463ae3a435ba51e303f5654bb1a,
title = "Role of Amino Acid Residues for Dioxygen Activation in the Second Coordination Sphere of the Dicopper Site of pMMO",
abstract = "Formation of an active oxygen species at the dicopper site of pMMO is studied by using density functional theory (DFT) calculations. The role of the amino acid residues of tyrosine (Tyr374) and glutamate (Glu35) located in the second coordination sphere of the dicopper site is discussed in detail. The phenolic proton of the tyrosine residue is transferred to the Cu2O2 core in a two-step manner via the glutamate residue, and an electron is directly transferred to the Cu2O2 core. These proton- and electron-transfer processes induce the O-O bond cleavage of the μ-η2:η2-peroxodicopper(II) species to form the (μ-oxo)(μ-hydroxo)CuIICuIII species, which is able to play a key role of methane hydroxylation at the dicopper site of pMMO ( Inorg. Chem. 2013 , 52 , 7907 ). This proton-coupled electron-transfer mechanism is a little different from that in tyrosinase in that the proton of substrate tyrosine is directly transferred to the dicopper site ( J. Am. Chem. Soc. 2006 , 128 , 9873 ) because there is no proton acceptor in the vicinity of the dicopper site of tyrosinase. The rate-determining step for the formation of the (μ-oxo)(μ-hydroxo)CuIICuIII species is determined to be the O-O bond cleavage. These results shed new light on the interpretation of the role of the tyrosine and glutamate residues located in the second coordination sphere of the dicopper site of pMMO.",
author = "Mayuko Miyanishi and Tsukasa Abe and Yuta Hori and Yoshihito Shiota and Kazunari Yoshizawa",
year = "2019",
month = "9",
day = "16",
doi = "10.1021/acs.inorgchem.9b01752",
language = "English",
volume = "58",
pages = "12280--12288",
journal = "Inorganic Chemistry",
issn = "0020-1669",
publisher = "American Chemical Society",
number = "18",

}

TY - JOUR

T1 - Role of Amino Acid Residues for Dioxygen Activation in the Second Coordination Sphere of the Dicopper Site of pMMO

AU - Miyanishi, Mayuko

AU - Abe, Tsukasa

AU - Hori, Yuta

AU - Shiota, Yoshihito

AU - Yoshizawa, Kazunari

PY - 2019/9/16

Y1 - 2019/9/16

N2 - Formation of an active oxygen species at the dicopper site of pMMO is studied by using density functional theory (DFT) calculations. The role of the amino acid residues of tyrosine (Tyr374) and glutamate (Glu35) located in the second coordination sphere of the dicopper site is discussed in detail. The phenolic proton of the tyrosine residue is transferred to the Cu2O2 core in a two-step manner via the glutamate residue, and an electron is directly transferred to the Cu2O2 core. These proton- and electron-transfer processes induce the O-O bond cleavage of the μ-η2:η2-peroxodicopper(II) species to form the (μ-oxo)(μ-hydroxo)CuIICuIII species, which is able to play a key role of methane hydroxylation at the dicopper site of pMMO ( Inorg. Chem. 2013 , 52 , 7907 ). This proton-coupled electron-transfer mechanism is a little different from that in tyrosinase in that the proton of substrate tyrosine is directly transferred to the dicopper site ( J. Am. Chem. Soc. 2006 , 128 , 9873 ) because there is no proton acceptor in the vicinity of the dicopper site of tyrosinase. The rate-determining step for the formation of the (μ-oxo)(μ-hydroxo)CuIICuIII species is determined to be the O-O bond cleavage. These results shed new light on the interpretation of the role of the tyrosine and glutamate residues located in the second coordination sphere of the dicopper site of pMMO.

AB - Formation of an active oxygen species at the dicopper site of pMMO is studied by using density functional theory (DFT) calculations. The role of the amino acid residues of tyrosine (Tyr374) and glutamate (Glu35) located in the second coordination sphere of the dicopper site is discussed in detail. The phenolic proton of the tyrosine residue is transferred to the Cu2O2 core in a two-step manner via the glutamate residue, and an electron is directly transferred to the Cu2O2 core. These proton- and electron-transfer processes induce the O-O bond cleavage of the μ-η2:η2-peroxodicopper(II) species to form the (μ-oxo)(μ-hydroxo)CuIICuIII species, which is able to play a key role of methane hydroxylation at the dicopper site of pMMO ( Inorg. Chem. 2013 , 52 , 7907 ). This proton-coupled electron-transfer mechanism is a little different from that in tyrosinase in that the proton of substrate tyrosine is directly transferred to the dicopper site ( J. Am. Chem. Soc. 2006 , 128 , 9873 ) because there is no proton acceptor in the vicinity of the dicopper site of tyrosinase. The rate-determining step for the formation of the (μ-oxo)(μ-hydroxo)CuIICuIII species is determined to be the O-O bond cleavage. These results shed new light on the interpretation of the role of the tyrosine and glutamate residues located in the second coordination sphere of the dicopper site of pMMO.

UR - http://www.scopus.com/inward/record.url?scp=85072233545&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85072233545&partnerID=8YFLogxK

U2 - 10.1021/acs.inorgchem.9b01752

DO - 10.1021/acs.inorgchem.9b01752

M3 - Article

C2 - 31464432

AN - SCOPUS:85072233545

VL - 58

SP - 12280

EP - 12288

JO - Inorganic Chemistry

JF - Inorganic Chemistry

SN - 0020-1669

IS - 18

ER -