Resonance Raman spectra of blue copper proteins: assignments from normal mode calculations and copper-63/copper-65 and H2O/D2O shifts for stellacyanin and laccase

Nestor, Lisa; Larrabee, James A.; Woolery, G. L.; Reinhammar, Bengt; Spiro, Thomas G.

doi:10.1021/bi00301a008

Cited by 76 publications

(113 citation statements)

References 66 publications

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“…The observed shift of the 281-cm-' peak in the M44K-azurin RR spectrum by +4 cm-' (Fig. 5 ) indicates an additional slight shortening of the Cu-N(His) bond(s) (Nestor et al, 1984;Blair et al, 1985) at pH 10 relative to pH 8. The lack of a change in the rest of the spectrum shows that there is no change in the geometry of the Cu-cysteinate moiety at high pH.…”

Section: Spectroscopic Effects Of Lys44 Deprotonationmentioning

confidence: 92%

“…5). The occurrence of such a large number of spectral features is due to kinematic coupling of the Cu-S(Cys) stretch with vibrational motions of the cysteine and histidine ligands (Nestor et al, 1984;Blair et al, 1985;Han et al, 1991). The frequencies and intensities in the RR spectra of wt and M44K azurin at pH 8.0 are similar ( (1) azurin (Canters et al, 1984a;.…”

Section: Resonance Raman Spectroscopymentioning

confidence: 99%

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Effect of lysine ionization on the structure and electrochemical behaviour of the Met44→Lys mutant of the blue‐copper protein azurin from Pseudomonas aeruginosa

Kamp

Canters

Andrew

et al. 1993

European Journal of Biochemistry

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The structural and spectrochemical effects of the replacement of Met44 in the hydrophobic surface patch of azurin from Pseudomonas aeruginosa by a lysine residue were studied as a function of the ionization state of the lysine. In the pH range 5 -8, the optical absorption, resonance Raman, EPR and electron spin-echo envelope modulation spectroscopic properties of wild-type and Met44-+Lys (M44K) azurin are very similar, indicating that the Cu-site geometry has been maintained. At higher pH, the deprotonation of Lys44 in M44K azurin (pK, 9-10) is accompanied by changes in the optical-absorption maxima (614 nm and 450 nm instead of 625 nm and 470 nm) and in the EPR gll value (2.298 instead of 2.241), indicative of a change in the bonding interactions of Cu at high pH. The strong pH dependence of the electron self-exchange rate of M44K azurin supports the assignment of Lys44 as the ionizable group and demonstrates the importance of the hydrophobic patch for electron transfer. The pH dependence of the midpoint potentials of wild-type and M44K azurin can be accounted for by the ionizations of His35 and His83 and by the additional electrostatic effect of the mutation.Electrostatic interactions have an important role in the determination of both the structure and function of proteins (Warshel and Russel, 1984;Davis and McCammon, 1990;Bashford, 1991). In the case of redox proteins, electrostatic interactions have a marked influence, e.g. on the midpoint potential (Rees, 1985;Moore et al., 1986). In this connection, the engineering of charged residues can be of particular interest, as it may lead to distinctly interpretable effects (Sternberg et al., 1987;Cutler et al., 1989;Varadarajan et al., 1989;Rodgers and Sligar, 1991). In this study, the effects of the replacement of the uncharged residue Met44 of the blue-copper protein azurin from Pseudomonas aeruginosa by a lysine residue (Van de Kamp et al., 1990a, b) on the electron self-exchange (ESE) rate constant (kESE), the spectroscopic and electrochemical properties, as well as their pH dependence, are reported (for reviews on blue-copper proteins see Adman, 1991 ;Sykes, 1991 ;Solomon et al., 1992).Met44 is located in the so-called hydrophobic surface patch of azurin (Nar et al., 1991 a, b; Fig. 1). This patch covers the type-] Cu site of azurin, the Cu ion being located at approximately 0.7 nm below the surface. The Cu-ligand resi- due His117 is located in the centre of this patch. The replacement of Met44 by the protonated lysine residue hardly affects the spectroscopic properties of the Cu site, but causes a considerable decrease of the k,,, value of azurin. At pH >8, deprotonation of Lys44 produces a new type-] Cu site, whereas the magnitude of the k,,, value of the protein is largely restored. At pH 5 and pH 8, the midpoint potential, Em, of Met44+Lys (M44K) MATERIALS AND METHODSIsolation and purification of azurin P. aeruginosa wt azurin was isolated from Escherichia coli as described (Van de Kamp et al., 1990~). The M44K mutant of azurin was isolated from E. cot...

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Section: Spectroscopic Effects Of Lys44 Deprotonationmentioning

confidence: 92%

Section: Resonance Raman Spectroscopymentioning

confidence: 99%

Effect of lysine ionization on the structure and electrochemical behaviour of the Met44→Lys mutant of the blue‐copper protein azurin from Pseudomonas aeruginosa

Kamp

Canters

Andrew

et al. 1993

European Journal of Biochemistry

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“…En effet, certains chercheurs supposent que les phytochélatines forment des complexes avec le cuivre à l'aide principalement des groupes sulfurés des acides aminés de cystéine (De Vos et al, 1992;Speiser et al, 1992;Dave et al, 1993). D'autres chercheurs ont remarqué que la complexation pourrait s'effectuer à partir des groupes NH 2 de certains acides aminés (Rao, 1963;Nestor et al, 1984;Sykes, 1991) et les groupes carboxyliques COOH (Strand et Jakobsen, 1991;Jackson et Mantsh, 1995). Les acides aminés de ces phytochélatines sont principalement la glutamine, la cystéine, la glycine et, à un degré moindre, l'histidine.…”

Section: Remerciementsunclassified

“…Une étude sur les levures Schizosaccharomyces pombe exposées au cadmium a montré que le composé y-glutamylcystéine est lié par la liaison cadmium-thiol (Plocke et Kâgi, 1992). Ce phénomène s'explique par le fait que la coordination avec le métal est souvent due à l'atome de soufre issu de la structure régulière tetraédrique CdS4 (Plocke et Kàgi, 1992 Nestor et al(1984) ainsi que Woodruff et al(1984) ont montré que le cuivre s'est lié à l'histidine grâce à la liaison N-H ayant comme structure Cu-N-histidine. À la suite des études citées antérieurement sur l'interaction métal-phytochélatines, nous ne pouvons associer l'interaction Cu-protéine juste au groupe thiol mais aussi aux groupes amides des acides aminés.…”

Section: Remerciementsunclassified

Caractérisation par spectroscopie infrarouge des complexes phytochélatines-cuivre chez Scenedesmus quadricauda /

Triki¹

1997

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“…Here we show details of the direct electrochemistry of stellacyanin. Few kinetic studies have been performed on stellacyanin [41-451 compared to a variety of optical and magnetic studies [8,[46][47][48][49].…”

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confidence: 99%

Electron transfer reaction of stellacyanin at a bare glassy carbon electrode

Ikeda

Sakurai

1994

European Journal of Biochemistry

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Direct (unmediated) electrochemistry of Rhus verniciferu stellacyanin at a glassy carbon electrode has been briefly investigated in phosphate buffer. The voltammetry was practically independent of the buffer concentration, suggesting that the interaction between stellacyanin and the glassy carbon electrode is mainly realized through the hydrophobic interaction. The quasi-reversible process was found to be diffusion controlled at a sweep rate < 80 mVs-I. From stellacyanin concentration dependence, a transformation from linear diffusion to radial diffusion was observed. Twostep voltammetry was affected by translocations of the active site (rotation of the protein molecule on the electrode surface and diffusion). Activation energies for reduction and oxidation processes were determined to be 24kJmol-' and 54k.Tmol-l, respectively, by the stationary method, and 15 k.Tmol-' and 66 Hmol-I, respectively, by cyclic voltammetry. The considerable difference in the activation energies is supposedly due to the reduction and oxidation which are performed utilizing different electron-transfer pathways or because only one electron-transfer pathway (probably through His92) is significantly changed during the reorganization between the oxidized and reduced forms. The fact that the diffusion constant estimated from one-step voltammetry (Dox= 4.2 X10-9 cm2 s-I for 484 pM stellacyanin) is much smaller than that determined from cyclic voltammetry (7.5X10-7 cm2 s-I) derives from the fact that motions of the stellacyanin molecule (rotation leading to translocation of the active site and diffusion) are not fast enough to allow data from potential step voltammetry to be treated as the reversible process, but are fast enough to allow data from cyclic voltammetry to be treated as a diffusion-controlled process.The electron-transfer reaction has received special attention for more than fifty years, since it is involved in important biological processes such as photosynthesis and respiration [l-41. Many of the studies have focused on revealing how the electron-transfer chains are constituted by the relevant proteins, how the redox couple recognize each other, and how the intermolecular and intramolecular electron transfers take place.The rate of the biological electron-transfer processes depends on an interplay of several factors such as the distance between the donor and acceptor, their orientation with respect to each other, the nature of the intervening medium and the groups involved in the transfer pathway, the thermodynamic driving force, and atomic motions coupled with electron transfer [ 5 ] .Together with cytochromes and iron-sulfur proteins, blue copper proteins also play a role in biological electron transfers [6, 71. This type of metalloprotein contains only oneCorrespondence to

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Resonance Raman spectra of blue copper proteins: assignments from normal mode calculations and copper-63/copper-65 and H2O/D2O shifts for stellacyanin and laccase

Cited by 76 publications

References 66 publications

Effect of lysine ionization on the structure and electrochemical behaviour of the Met44→Lys mutant of the blue‐copper protein azurin from Pseudomonas aeruginosa

Effect of lysine ionization on the structure and electrochemical behaviour of the Met44→Lys mutant of the blue‐copper protein azurin from Pseudomonas aeruginosa

Caractérisation par spectroscopie infrarouge des complexes phytochélatines-cuivre chez Scenedesmus quadricauda /

Electron transfer reaction of stellacyanin at a bare glassy carbon electrode

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