Further perspectives on the charge transfer transitions of blue copper proteins and the ligand moieties in stellacyanin

McMillin, David R.; Morris, Margaret C.

doi:10.1073/pnas.78.11.6567

Cited by 30 publications

(14 citation statements)

References 28 publications

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“…Multiple (strong and weak) Au binding sites in BSA has also been suggested by others . A plausible origin of the red fluorophore could involve, ligand field (LF), ligand-to-metal charge transfer (LMCT), and/or metal-to-ligand charge transfer (MLCT) transition, − although the details of the local coordination at the Cys–Cys binding sites are needed to understand the mechanism. Alternatively, strong electron delocalization can occur at aromatic residue(s) among at least one of the Sites I – IX , for example via dehydration or cyclization. − However, it is unclear whether such processes can be mediated by Au(III).…”

Section: Resultsmentioning

confidence: 86%

Conformational Change-Induced Fluorescence of Bovine Serum Albumin–Gold Complexes

Dixon

Egusa

2018

J. Am. Chem. Soc.

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We report new findings on the red fluorescent (λ = 640 nm) bovine serum albumin (BSA)-gold (Au) compound initially described by Xie et al. (J. Am. Chem. Soc. 2009, 131, 888-889) as Au nanoclusters. The BSA-Au compounds were further reducible to yield nanoparticles, suggesting that these compounds were BSA-cationic Au complexes. We examined the correlations between BSA conformations (pH-induced as well as denatured) and the resulting fluorescence of BSA-Au complexes, to understand the possible cationic Au binding sites. The red fluorescence of the BSA-Au complex was associated with a particular isoform of BSA, the aged form (pH > 10) of the five pH-dependent BSA conformations, while the other conformations, expanded (pH < 2.7), fast (2.7 < pH < 4.3), normal (4.3 < pH < 8), and basic (8 < pH < 10) did not result in red fluorescence. There could be internal energy transfer mechanisms to produce red fluorescence, deduced from excitation-emission map measurements. The ensemble minimum number of Au(III) per BSA to yield red fluorescence was <7. We illustrate the presence of multiple specific Au binding sites in BSA, and present an interpretation of the fluorescence of the BSA-Au complex, alternative to a single-site nucleation of a neutral Au nanocluster.

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Section: Resultsmentioning

confidence: 86%

Conformational Change-Induced Fluorescence of Bovine Serum Albumin–Gold Complexes

Dixon

Egusa

2018

J. Am. Chem. Soc.

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“…8 the low temperature (T--20 K) visible spectrum is reported, together with the fitting in terms of Gaussian components. Four bands, attributed to ligand to metal charge transfer transitions, are expected (Solomon et al 1980;McMillin and Morris 1981;Gewirth and Solomon 1988) and, indeed, four Gaussian components (labeled I to IV in Fig. 8) are needed to fit the spectrum.…”

Section: H(v) C 2 H(v) Mg=acoth~+mentioning

confidence: 99%

Low temperature optical absorption spectroscopy: an approach to the study of stereodynamic properties of hemeproteins

et al. 1995

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In this short review we show how suitable analysis of the temperature dependence of the optical absorption spectra of metalloproteins can give insight into their stereodynamic properties in the region of the chromophore. To this end, the theory of coupling between an intense allowed electronic transition of a chromophore and Franck-Condon active vibrations of the nearby atoms is applied to the Soret band of hemeproteins to obtain an analytical expression suitable for fitting the spectral profile at various temperatures. The reported approach enables one to separate the various contributions to the overall bandwidth together with the parameters that characterize the vibrational coupling. The thermal behavior of these quantities gives information on the dynamic properties of the active site and on their dependence upon protein structure and ligation state. The Soret band of hemeproteins appears to be coupled to high frequency vibrational modes of the heme group (as already shown by resonance Raman spectroscopy) and to a "bath" of low frequency modes most likely deriving from the bulk of the protein. For the deoxy derivatives inhomogeneous broadening arising from conformational heterogeneity appears to contribute substantially to the linewidth. The data indicate the onset, at temperatures near 180 K, of large scale anharmonic motions that can be attributed to jumping among different conformational substates of the protein.

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“…St however lacks this amino acid. On the basis of spectral analysis, McMillin and co-workers (Tennent & McMillin, 1979;McMillin & Morris, 1981) have therefore suggested that the fourth ligand in stellacyanin may be a disulfide sulfur. A similar suggestion has been made by Ferris et al (1978), who analyzed the resonance Raman spectra of stellacyanin.…”

Section: Resultsmentioning

confidence: 99%

Electron-transfer pathways in stellacyanin: a possible homology with plastocyanin

Farver¹,

Licht²,

Pecht³

1987

Biochemistry

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Further perspectives on the charge transfer transitions of blue copper proteins and the ligand moieties in stellacyanin

Cited by 30 publications

References 28 publications

Conformational Change-Induced Fluorescence of Bovine Serum Albumin–Gold Complexes

Conformational Change-Induced Fluorescence of Bovine Serum Albumin–Gold Complexes

Low temperature optical absorption spectroscopy: an approach to the study of stereodynamic properties of hemeproteins

Electron-transfer pathways in stellacyanin: a possible homology with plastocyanin

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