Surface-enhanced Raman scattering of cytochromes c3 adsorbed on silver electrode and their redox behavior

Niki, Katsumi; Kawasaki, Yoshikane; Kimura, Yasuhiro; Higuchi, Youichi; Yasuoka, Noritake

doi:10.1021/la00078a018

Cited by 42 publications

(17 citation statements)

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“…As a result of these unique structural features, the Cc3 exhibit a number of unusual physiochemical properties. The reduction potentials of the four Cc3 heme groups are very low, resulting in macroscopic reduction po-tentials linking the five macroscopic oxidation states of Cc3 that range from -240 to -357 mV vs. NHE for Cc3 from Desulfovibrio vulgaris Miyazaki F (Niki et al, 1987). Solid films of reduced Cc3 exhibit a very high conductance (Kimura et al, 1979;Nakahara et al, 1980), a property which may provide useful applications for Cc3 in bioelectronics.…”

Section: Introductionmentioning

confidence: 99%

Time-resolved absorption and magnetic circular dichroism spectroscopy of cytochrome c3 from Desulfovibrio

O'Connor

Goldbeck

Hazzard

et al. 1993

Biophysical Journal

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The UV-visible absorption and magnetic circular dichroism (MCD) spectra of the ferric, ferrous, CO-ligated forms and kinetic photolysis intermediates of the tetraheme electron-transfer protein cytochrome c3 (Cc3) are reported. Consistent with bis-histidinyl axial coordination of the hemes in this Class III c-type cytochrome, the Soret and visible region MCD spectra of ferric and ferrous Cc3 are very similar to those of other bis-histidine axially coordinated hemeproteins such as cytochrome b5. The MCD spectra indicate low spin state for both the ferric (S = 1/2) and ferrous (S = 0) oxidation states. CO replaces histidine as the axial sixth ligand at each heme site, forming a low-spin complex with an MCD spectrum similar to that of myoglobin-CO. Photodissociation of Cc3-CO (observed photolysis yield = 30%) produces a transient five-coordinate, high-spin (S = 2) species with an MCD spectrum similar to deoxymyoglobin. The recombination kinetics of CO with heme Fe are complex and appear to involve at least five first-order or pseudo first-order rate processes, corresponding to time constants of 5.7 microseconds, 62 microseconds, 425 microseconds, 2.9 ms, and a time constant greater than 1 s. The observed rate constants were insensitive to variation of the actinic photon flux, suggesting noncooperative heme-CO rebinding. The growing in of an MCD signal characteristic of bis-histidine axial ligation within tens of microseconds after photodissociation shows that, although heme-CO binding is thermodynamically favored at 1 atm CO, binding of histidine to the sixth axial site competes kinetically with CO rebinding.

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Section: Introductionmentioning

confidence: 99%

Time-resolved absorption and magnetic circular dichroism spectroscopy of cytochrome c3 from Desulfovibrio

O'Connor

Goldbeck

Hazzard

et al. 1993

Biophysical Journal

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“…These techniques selectively probe the vibrational structure of the heine chromophore, yielding information on the conformation of the heme and its interactions with the immediate protein environment (Cotton et al 1980;Spiro 1983;Smulevich and Spiro 1985;de Groot and Hester 1987;Kitagawa and Ozaki 1987;Wolf et al 1988;Niki et al 1989;Verma et al 1989). A detailed analysis was carried out for cyt c adsorbed at the silver electrode/electrolyte interface (Hildebrandt and Stockburger 1989a).…”

Section: Introductionmentioning

confidence: 99%

Quantitative conformational analysis of cytochromec bound to phospholipid vesicles studied by resonance Raman spectroscopy

1990

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Resonance Raman spectra have been recorded from ferri-cytochrome c bound to phospholipid vesicles composed of dimyristoyl phosphatidylglycerol (DMPG), dioleoyl phosphatidylglycerol (DOPG) or dioleoyl phosphatidylglycerol-dioleoyl phosphatidylcholine (DOPG-DOPC) (70:30 mole/mole). Lipid binding induces very significant conformational changes in the protein molecule. The resonance Raman spectra differ in their content of bands originating from two different conformational species, I and II, of the protein, and from two different spin and coordination states of the heme in conformation II. Data of sufficiently high precision were obtained that the spectra of the individual species could be quantitated by a constraint interactive fitting routine using single Lorentzian profiles. In the high frequency, or marker band region (1200 to 1700 cm-1), the frequencies, half widths and relative intensities of the individual bands could be estimated from previous surface enhanced resonance Raman measurements on cytochrome c adsorbed on a silver electrode. These were then further optimized to yield both the spectral parameters and relative contents of the different species. In the low frequency, or fingerprint, region (200 to 800 cm-1), the spectral parameters of the individual species were obtained from difference spectra derived by sequential subtraction between the spectra of ferri-cytochrome c in the three different lipid systems, using the relative proportions of the species derived from the marker band region. These parameters were then subsequently refined by iterative optimization. The optimized spectral parameters in both frequency regions for the six-coordinated low spin states I and II, and for the five-coordinated high spin state II are presented.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…Proteins such as Cytochrome c (Cyt c), Hemoglobin (Hb), glucose oxidase, lactate oxidase, and flavoproteins have been thoroughly studied. 18,–22 Perhaps due to the difficulties of obtaining a reasonable and rich spectrum, most of the early reports focused on proteins with a heme group and employed SERRS to benefit from additional resonance enhancement. Silver electrodes or colloidal silver nanoparticles (AgNPs) were used as substrates in almost all of these studies.…”

Section: Sers and Proteinsmentioning

confidence: 99%

Surface-Enhanced Raman Scattering: An Emerging Label-Free Detection and Identification Technique for Proteins

Çulha

2013

Appl Spectrosc

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The detection and identification of biologically important molecules has critical importance in several fields such as medicine, biotechnology, and pharmacology. Surface-enhanced Raman scattering (SERS) is a powerful emerging vibrational spectroscopic technique that allows not only for the characterization, but also for the identification and detection of biomacromolecules in a very short time. In this review, efforts to utilize SERS for label-free protein detection and identification is summarized after a short introduction of proteins and the technique.

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Surface-enhanced Raman scattering of cytochromes c3 adsorbed on silver electrode and their redox behavior

Cited by 42 publications

References 1 publication

Time-resolved absorption and magnetic circular dichroism spectroscopy of cytochrome c3 from Desulfovibrio

Time-resolved absorption and magnetic circular dichroism spectroscopy of cytochrome c3 from Desulfovibrio

Quantitative conformational analysis of cytochromec bound to phospholipid vesicles studied by resonance Raman spectroscopy

Surface-Enhanced Raman Scattering: An Emerging Label-Free Detection and Identification Technique for Proteins

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