Connection between Structure, Electronic Spectrum, and Electron-Transfer Properties of Blue Copper Proteins

Larsson, Sven; Broo, Anders; Sjoelin, Lennart

doi:10.1021/j100013a067

Cited by 89 publications

(115 citation statements)

References 12 publications

Supporting

Mentioning

102

Contrasting

Order By: Relevance

“…Larsson et al have reported semiempirical CNDO/S calculations of the active site of azurin. 20 An intense band was predicted to lie at 13 800 cm À1 , and in agreement with Solomon was assigned to excitations from the bonding Cu 3d-S cys 3p p orbital. Contrary to the earlier work, ligand field excitations were found at higher energy.…”

Section: Introductionsupporting

confidence: 61%

Modelling the spectroscopy and dynamics of plastocyanin

Robinson

Besley

2010

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

The electronic absorption, electronic circular dichroism and X-ray absorption spectroscopy of the blue copper protein plastocyanin is studied with density functional theory, time-dependent density functional theory and multireference configuration interaction in conjunction with classical molecular dynamics simulations. A strong correlation is observed between the excitation energy of the intense ligand to metal charge transfer band and the copper-cysteine sulfur bond length. The results suggest that the copper-cysteine sulfur bond length in the crystal structure of plastocyanin is too short and should be closer to the corresponding bond lengths in related blue copper proteins. Averaging over many structural conformations is required to reproduce the major features of the experimental circular dichroism spectra. A correlation between the rotational strength of the ligand to metal charge transfer band and the distortion of the copper atom from the plane of the cysteine sulfur and histidine nitrogen atoms is found. X-ray absorption calculations show a smaller sulfur p orbital character in the singly occupied molecular orbital of cucumber basic protein compared to plastocyanin.

show abstract

Section: Introductionsupporting

confidence: 61%

Modelling the spectroscopy and dynamics of plastocyanin

Robinson

Besley

2010

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

show abstract

“…8 Semiempirical electronic-structure calculations have indicated, however, that little charge redistribution actually occurs in this transition, so this characterization may be misleading. 9,10 The weaker peak at 770 nm is a combination of three transitions from filled copper d orbitals to the half-filled d 11 The most widely studied blue copper protein is plastocyanin, a small (10.5 kDa) photosynthetic protein of plants, algae, and cyanobacteria that transfers an electron from cytochrome f in photosystem II to a chlorophyll in photosystem I. 12 Although a plastocyanin protein contains a single copper center, many proteins in this class contain several copper atoms, some of which may not be bound to active sites of the blue type I configuration.…”

Section: Introductionmentioning

confidence: 99%

“…17a The fact that most of the resonance-enhanced modes involve the Cu-S(cysteine) stretch can be rationalized from the results of semiempirical calculations, which show that the electronic excitation is localized around this bond. 9,10 Thus, it is expected that this bond will undergo the most distortion upon excitation. 16 Solomon et al have suggested that the Cu-S(cysteine) bond plays a key role in the physiological electronic-transfer event.…”

Section: Introductionmentioning

confidence: 99%

Ultrafast Pump−Probe Studies of Excited-State Charge-Transfer Dynamics in Blue Copper Proteins

Book

Arnett

et al. 1998

J. Phys. Chem. A

View full text Add to dashboard Cite

We report the results of ultrafast pump-probe measurements on three blue copper proteins: spinach plastocyanin, poplar plastocyanin, and human ceruloplasmin. Electronic population dynamics and vibrational coherences involving d f d transitions of the blue copper active site are observed using both wavelengthintegrated and wavelength-resolved detection. Depending on the protein and the method of detection, the pump-induced bleaches of the electronic ground state decay with time constants of 230-300 fs. The pumpprobe signals are modulated by oscillations that correspond to vibrational coherences induced by the ultrashort pulses. The frequencies of some of these oscillations can be matched with modes observed in resonance Raman studies of these proteins. For spinach plastocyanin and ceruloplasmin, wavelength-resolved signals reveal a previously unreported vibration at ∼500 cm -1 whose decay dynamics are consistent with the excitedstate lifetime. The origin of this mode is argued to result from Duschinsky rotation. The relevance of these pump-probe results to the development of a model for biological electron transport in these proteins is discussed.

show abstract

“…Plastocyanin indicates intense absorption band due to the S Cys 3 Cu(II) charge transfer at visible region and a narrow hyperfine coupling constant in the EPR spectra of the oxidized form (2). The electronic structure of plastocyanin has been reported by several groups (3)(4)(5). Solomon and co-workers (6) gave an implication for the electron transfer reaction mechanisms on the basis of the electronic structure of plastocyanin.…”

mentioning

confidence: 99%

The Structure and Unusual pH Dependence of Plastocyanin from the Fern Dryopteris crassirhizoma

Kohzuma¹,

Inoue²,

Yoshizaki³

et al. 1999

Journal of Biological Chemistry

114

View full text Add to dashboard Cite

Spectroscopic properties, amino acid sequence, electron transfer kinetics, and crystal structures of the oxidized (at 1.7 Å resolution) and reduced form (at 1.8 Å resolution) of a novel plastocyanin from the fern Dryopteris crassirhizoma are presented. Kinetic studies show that the reduced form of Dryopteris plastocyanin remains redox-active at low pH, under conditions where the oxidation of the reduced form of other plastocyanins is inhibited by the protonation of a solvent-exposed active site residue, His 87 (equivalent to His 90 in Dryopteris plastocyanin). The x-ray crystal structure analysis of Dryopteris plastocyanin reveals -stacking between Phe 12 and His 90 , suggesting that the active site is uniquely protected against inactivation. Like higher plant plastocyanins, Dryopteris plastocyanin has an acidic patch, but this patch is located closer to the solvent-exposed active site His residue, and the total number of acidic residues is smaller. In the reactions of Dryopteris plastocyanin with inorganic redox reagents, the acidic patch (the "remote" site) and the hydrophobic patch surrounding His 90 (the "adjacent" site) are equally efficient for electron transfer. These results indicate the significance of the lack of protonation at the active site of Dryopteris plastocyanin, the equivalence of the two electron transfer sites in this protein, and a possibility of obtaining a novel insight into the photosynthetic electron transfer system of the first vascular plant fern, including its molecular evolutionary aspects. This is the first report on the characterization of plastocyanin and the first three-dimensional protein structure from fern plant.

show abstract

Connection between Structure, Electronic Spectrum, and Electron-Transfer Properties of Blue Copper Proteins

Cited by 89 publications

References 12 publications

Modelling the spectroscopy and dynamics of plastocyanin

Modelling the spectroscopy and dynamics of plastocyanin

Ultrafast Pump−Probe Studies of Excited-State Charge-Transfer Dynamics in Blue Copper Proteins

The Structure and Unusual pH Dependence of Plastocyanin from the Fern Dryopteris crassirhizoma

Contact Info

Product

Resources

About