Spectroscopic aspects of copper binding site in bovine serum amine oxidase

Suzuki, Shinnichiro; Sakurai, Takeshi; Nakahara, Akitsugu; Oda, Osamu; Manabe, Takashi; Okuyama, Tsuneo

doi:10.1016/0014-5793(80)80519-9

Cited by 26 publications

(12 citation statements)

References 22 publications

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“…The T2 Cu H site of PHM has a g z of 2.29 and an A z of 471 MHz . In processed AOs with the Cu(His) 3 (OH 2 ) 1–2 ligation, the g z values are found in the range of 2.28–2.32, while the A z varies between 480 and 561 MHz. ,− Furthermore, the superhyperfine splitting in the g ⊥ region of AO − and LPMO , has been observed with an A N of 13–14 G. These values are comparable to [3SCC-Cu(I9H) 3 ] 2+ . The lack of water ligation in the X-ray structure is intriguing, and it most likely indicates cryoreduction of Cu(II) to Cu(I) causing the water(s) to dissociate upon irradiation.…”

Section: Discussionmentioning

confidence: 59%

De Novo Design of a Self-Assembled Artificial Copper Peptide that Activates and Reduces Peroxide

et al. 2021

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Copper-containing metalloenzymes constitute a major class of proteins that catalyze a myriad of reactions in nature. Inspired by the structural and functional characteristics of this unique class of metalloenzymes, we report the conception, design, characterization, and functional studies of a de novo artificial copper peptide (ArCuP) within a trimeric self-assembled polypeptide scaffold that activates and reduces peroxide. Using a first-principles approach, the ArCuP was designed to coordinate one Cu via three His residues introduced at an a site of the peptide scaffold. X-ray crystallography, UV–vis, and electron paramagnetic resonance data demonstrate that Cu binds via the Nε atoms of His forming a T2Cu environment. When reacted with hydrogen peroxide, the putative copper-hydroperoxo species is formed where a reductive priming step accelerates the rate of its formation and reduction. Mass spectrometry was used to identify specific residues undergoing oxidative modification, which showed His oxidation only in the reduced state. The redox behavior of the ArCuP was elucidated by protein film voltammetry. Detailed characterization of the electrocatalytic behavior of the ArCuP led us to determine the catalytic parameters (K M and k cat), which established the peroxidase activity of the ArCuP. Combined spectroscopic and electrochemical data showed a pH dependence on the reactivity, which was optimum at pH 7.5.

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Section: Discussionmentioning

confidence: 59%

De Novo Design of a Self-Assembled Artificial Copper Peptide that Activates and Reduces Peroxide

et al. 2021

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“…This enzyme exhibits the yellow-pink color which results from a broad absorption band near 480 nm. Our previous spectral studies (Suzuki et al, 1980(Suzuki et al, , 1981(Suzuki et al, , 1982 of native, Co(II) substituted, and diethyl dithiocarbamate treated BSAO have partly clarified the coordination chemistry of the copper(II) and the apparent presence of an unknown organic prosthetic group. This paper describes more profound spectroscopic and chemical properties of the chromophore, the roles of copper ion, and the intimate correlation between the two cofactors in native BSAO, and its derivatives.…”

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confidence: 99%

Effect of metal substitution on the chromophore of bovine serum amine oxidase

Suzuki¹,

Sakurai²,

Nakahara³

et al. 1983

Biochemistry

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“…(Copper-containing amine oxidases [amine:oxygen oxidoreducíase (deaminating) (copper-containing), EC 1.4.3.6] catalyze the oxidative deamination of amines by accepting two electrons from amines and transferring them to molecular oxygen, as expressed by the equation (Malmstróm et al, 1975) RCH2NH2 + Oz + H20 -RCHO + NH3 + H202 They are known to contain nonblue and electron paramagnetic resonance (EPR)1 detectable copper (Yamada et al, , 1969Mondovi et al, 1967;Lindstróm et al, 1974;Suzuki et al, 1980Suzuki et al, , 1983) and an organic chromophore responsible for their yellowish pink color Lindstróm & Pettersson, 1973;Ishizaki & Yasunobu, 1976;Finazzi-Agro et al, 1977 et al, 1981, 1982, 1983). Reactions of the copper with complexing agents (Yamada & Yasunobu, 1962;Lindstróm & Pettersson, 1974;Lindstróm et al, 1974) or of the chromophore with carbonyl reagents Falk, 1983) lead to an inactivation of the enzyme.…”

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confidence: 99%

Roles of the two copper ions in bovine serum amine oxidase

Suzuki¹,

Sakurai²,

Nakahara³

et al. 1986

Biochemistry

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With a view to obtaining information on the roles of the two copper ions in bovine serum amine oxidase (BSAO), spectroscopic and magnetic studies on several BSAO derivatives have been carried out. Cu-depleted BSAO (Cu-depBSAO) exhibits no enzyme activity and only a low absorption intensity at ca. 475 nm, which is the characteristic absorption maximum of the chromophore in BSAO. The binding of 1 mol of Cu to 1 mol of Cu-depBSAO slightly but definitely increases the enzyme activity and the absorptivity, although they are much lower than those of native BSAO. The incorporation of 2 mol of Cu into Cu-depBSAO gives rise to a similar high activity and absorptivity as those of the native enzyme. Electron paramagnetic resonance (EPR) spectra of the BSAO derivatives reveal that two copper ions in the enzyme molecule are environmentally identical. Titrations of BSAO, Cu-depBSAO, and Cu-half-depleted BSAO (Cu-half-depBSAO), containing 1 mol of copper per mole of protein, with phenylhydrazine (an inhibitor of BSAO) indicate that only 1 mol of phenylhydrazine reacts with 1 mol of the enzyme. In other words the enzyme possesses only one chromophore or one active site, though the molecule is composed of two electrophoretically identical subunits. The binding constants between phenylhydrazine and BSAO, Cu-depBSAO, or Cu-half-depBSAO were estimated to be 5 X 10(6), 5 X 10(4), and 1 X 10(5) M-1, respectively. The binding of phenylhydrazine to the chromophore is assisted by the presence of two copper ions by a factor of 100.(ABSTRACT TRUNCATED AT 250 WORDS)

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Spectroscopic aspects of copper binding site in bovine serum amine oxidase

Cited by 26 publications

References 22 publications

De Novo Design of a Self-Assembled Artificial Copper Peptide that Activates and Reduces Peroxide

De Novo Design of a Self-Assembled Artificial Copper Peptide that Activates and Reduces Peroxide

Effect of metal substitution on the chromophore of bovine serum amine oxidase

Roles of the two copper ions in bovine serum amine oxidase

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