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Van Pouderoyen G, Andrew CR, Loehr TM, Sanders-Loehr J, Mazumdar S, Hill HA, Canters GW: Spectroscopic and mechanistic studies of type-1 and type-2 copper sites in Pseudomonas aeruginosa azurin as obtained by external ligands to mutant His46Gly. Biochemistry 1996, 35:1397-1407.
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Bauer R, Danielsen E, Hemmingsen L, Bjerrum MJ, Hansson Ö, Singh K: Interplay between oxidations state and coordination geometry of metal ions in azurin. J Am Chem Soc 1997, 119:157-162. This study employs a rather unusual method - perturbed angular correlation of γ-rays spectroscopy. This is the only copper protein study available using this method.
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Farver O, Skov LK, Young S, Bonander N, Karlsson BG, Vänngård T, Pecht I: Aromatic residues may enhance intramolecular electron transfer in azurin. J Am Chem Soc 1997, 119:5453-5454. This paper describes direct evidence for a role of aromatic residues in electron transfer in proteins.
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Sigfridsson K, Young S, Hansson Ö: Electron transfer between spinach plastocyanin mutants and photosystem 1. Eur J Biochem 1997, 245:805-812.
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Young S, Sigfridsson K, Olesen K, Hansson Ö: The involvement of two acidic patches of spinach plastocyanin in the reaction with photosystem 1. Biochim Biophys Acta 1997, 1322:106-114.
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Sigfridsson K, Sundahl M, Bjerrum MJ, Hansson Ö: Intraprotein electron transfer in a ruthenium-modified Tyr83-His plastocyanin mutant: evidence for strong electronic coupling. J Biol Inorg Chem 1996, 1:405-414.
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A and its dinuclear nature. Its dinuclear nature was resisted by some investigators as late as the spring of 1995, when, in the minds of most people in the field, it had already been established by analytical and spectroscopic data on soluble domains; it was not fully accepted until the crystal structures were published later in that year.
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Eur J Biochem
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3 subunit II from Thermus thermophilus. Biochemistry 1996, 35:3387-3395.
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Thermus Thermophilus. Biochemistry
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3 of Thermus thermophilus. Biophys J 1996, 71:2823-2829. In addition to its scientific significance, this paper describes a technically very elegant investigation, employing different Cu isotopes and several microwave frequencies as well electronic-structure calculations.
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Battistuzzi G, Borsari M, Loschi L, Sola M: Redox thermodynamics, acid-base equilibria and salt-induced effects for the cucumber basic protein. General implications for blue-copper proteins. J Biol Inorg Chem 1997, 2:350-359. This article gives a valuable discussion of the control of the reduction potentials of blue copper proteins in thermodynamic terms.
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A of cytochrome c oxidase, consistent with Cu-Cu bonding, and shows that there is very little change in these on reduction, accounting for the low reorganization energy.
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Prigge ST, Kolhekar AS, Eipper EA, Mains RE, Amzel LM: Amidation of bioactive peptides: the structure of peptidylglycine α-hydroxylating monooxygenase. Science 1997, 278:1300-1305. This paper describes the first structure determination of a member of this group of copper-containing oxygenases. The mechanistic knowledge extracted can be extrapolated to other members of the group, including dopamine β-monooxygenase.
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Halfen JA, Jazdzewski BA, Mahapatra S, Berreau LM, Wilkinson EC, Que L Jr, Tolman WB: Synthetic models of the inactive copper(II)-tyrosinate and active copper(II)-tyrosyl radical forms of galactose and glyoxal oxidases. J Am Chem Soc 1997, 119:8217-8227.
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Sokolowski A, Leutbecher H, Weyhermüller T, Schnepf R, Bothe E, Bill E, Hildebrandt P, Wieghardt K: Phenoxyl-copper(II) complexes: models for the active site of galactose oxidase. J Biol Inorg Chem 1997, 2:444-453.
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Gerfen GJ, Bellew BF, Griffin RG, Singel DJ, Ekberg CA, Whittaker JW: High-frequency electron paramagnetic resonance spectroscopy of the apogalactose oxidase radical. J Phys Chem 1996, 100:16739-16748.
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Wachter RM, Montague-Smith MP, Branchaud BP: β-haloethanol substrates as probes for radical mechanisms for galactose oxidase. J Am Chem Soc 1997, 119:7743-7749.
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