Abstract
Mössbauer spectroscopy was used to study the tetraheme cytochrome c3 from Desulfovibrio baculatus (DSM 1743). Samples with different degrees of reduction were prepared using a redoxtitration technique. In the reduced cytochrome c3, all four hemes are reduced and exhibit diamagnetic Mössbauer spectra typical for low‐spin ferrous hemes (S= 0). In the oxidized protein, the hemes are low‐spin ferric (S= 1/2) and exhibit overlapping magnetic Mössbauer spectra. A method of differential spectroscopy was applied to deconvolute the four overlapping heme spectra and a crystal‐field model was used for data analysis. Characteristic Mössbauer spectral components for each heme group are obtained. Hyperfine and crystal‐field parameters for all four hemes are determined from these deconvoluted spectra.
| Original language | English |
|---|---|
| Pages (from-to) | 779-782 |
| Number of pages | 4 |
| Journal | European Journal Of Biochemistry |
| Volume | 204 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1 Jan 1992 |
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Mössbauer characterization of the tetraheme cytochrome c3 from Desulfovibrio baculatus (DSM 1743): Spectral deconvolution of the heme components. / Ravi, Natarajan; Moura, Isabel; Costa, Cristina; Teixeira, Miguel; LeGALL, Jean; Moura, José J. G.; HUYNH, Boi Hanh.
In: European Journal Of Biochemistry, Vol. 204, No. 2, 01.01.1992, p. 779-782.Research output: Contribution to journal › Article
TY - JOUR
T1 - Mössbauer characterization of the tetraheme cytochrome c3 from Desulfovibrio baculatus (DSM 1743): Spectral deconvolution of the heme components
AU - Ravi, Natarajan
AU - Moura, Isabel
AU - Costa, Cristina
AU - Teixeira, Miguel
AU - LeGALL, Jean
AU - Moura, José J. G.
AU - HUYNH, Boi Hanh
N1 - NIGMS NIH HHS (GM 32187; GM 414821)
PY - 1992/1/1
Y1 - 1992/1/1
N2 - Mössbauer spectroscopy was used to study the tetraheme cytochrome c3 from Desulfovibrio baculatus (DSM 1743). Samples with different degrees of reduction were prepared using a redoxtitration technique. In the reduced cytochrome c3, all four hemes are reduced and exhibit diamagnetic Mössbauer spectra typical for low‐spin ferrous hemes (S= 0). In the oxidized protein, the hemes are low‐spin ferric (S= 1/2) and exhibit overlapping magnetic Mössbauer spectra. A method of differential spectroscopy was applied to deconvolute the four overlapping heme spectra and a crystal‐field model was used for data analysis. Characteristic Mössbauer spectral components for each heme group are obtained. Hyperfine and crystal‐field parameters for all four hemes are determined from these deconvoluted spectra.
AB - Mössbauer spectroscopy was used to study the tetraheme cytochrome c3 from Desulfovibrio baculatus (DSM 1743). Samples with different degrees of reduction were prepared using a redoxtitration technique. In the reduced cytochrome c3, all four hemes are reduced and exhibit diamagnetic Mössbauer spectra typical for low‐spin ferrous hemes (S= 0). In the oxidized protein, the hemes are low‐spin ferric (S= 1/2) and exhibit overlapping magnetic Mössbauer spectra. A method of differential spectroscopy was applied to deconvolute the four overlapping heme spectra and a crystal‐field model was used for data analysis. Characteristic Mössbauer spectral components for each heme group are obtained. Hyperfine and crystal‐field parameters for all four hemes are determined from these deconvoluted spectra.
UR - http://www.scopus.com/inward/record.url?scp=0026610351&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1992.tb16694.x
DO - 10.1111/j.1432-1033.1992.tb16694.x
M3 - Article
VL - 204
SP - 779
EP - 782
JO - European Journal Of Biochemistry
JF - European Journal Of Biochemistry
SN - 0014-2956
IS - 2
ER -