Characterization of zinc-substituted cytochrome c by circular dichroism and resonance Raman spectroscopic methods

Ye, Shuyu; Shen, Chengyu; Cotton, Therese M.; Kostić, Nenad M.

doi:10.1016/s0162-0134(97)00001-9

Cited by 44 publications

(65 citation statements)

References 68 publications

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“…These were bound approximately four times more tightly than PPIX itself. All three metals that we examined in this study (iron, copper, and zinc) can bind to the histidine within the active site in heme-proteins (1,47,55). The observation that these metalloprotoporphyrins bind to HmuR somewhat better than PPIX itself is consistent with a histidine in HmuR serving as the axial ligand, which binds to the metal ion present in the porphyrin ring.…”

Section: Discussionsupporting

confidence: 56%

Binding Specificity of the Porphyromonas gingivalis Heme and Hemoglobin Receptor HmuR, Gingipain K, and Gingipain R1 for Heme, Porphyrins, and Metalloporphyrins

2001

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Previous genetic and biochemical studies have confirmed that hemoglobin and hemin utilization in Porphyromonas gingivalis is mediated by the outer membrane hemoglobin and heme receptor HmuR, as well as gingipain K (Kgp), a lysine-specific cysteine protease, and gingipain R1 (HRgpA), one of two arginine-specific cysteine proteases. In this study we report on the binding specificity of the recombinant P. gingivalis HmuR protein and native gingipains for hemoglobin, hemin, various porphyrins, and metalloporphyrins as assessed by spectrophotometric assays, by affinity chromatography, and by enzyme-linked immunosorbent assay. Protoporphyrin, mesoporphyrin, deuteroporphyrin, hematoporphyrin, and some of their iron, copper, and zinc derivatives were examined to evaluate the

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Section: Discussionsupporting

confidence: 56%

Binding Specificity of the Porphyromonas gingivalis Heme and Hemoglobin Receptor HmuR, Gingipain K, and Gingipain R1 for Heme, Porphyrins, and Metalloporphyrins

2001

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“…No x-ray structure is available for MPl 1 and the 2.00 A value obtained from the MP11 Raman data shows that the core size of the undecapeptide not only approximates that of its parent but also indirectly confirms the presence of a 6th ligand: Ye et al (41) have recently shown that a cytochrome c core size is expected to be 2.025A when the metal is six-coordinate and our correlation yields a very close value. Such a core size value also suggests that the non-planarity of the heme of cytochrome c is conserved in the undecapeptide (42,43).…”

Section: Porphyrin Core Size and Planaritysupporting

confidence: 60%

Microperoxidase-11: Molecular Dynamics and Q-Band Excited Resonance Raman of the Oxidized, Reduced and Carbonyl Forms

Laberge

Vreugdenhil

Vanderkooi

et al. 1998

Journal of Biomolecular Structure and Dynamics

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Resonance Raman spectra with Q-band excitation are reported for microperoxidase-11, the cytochrome c analog. Spectra were acquired in the mid-frequency range for the oxidized, and reduced forms of the undecapeptide, as well as for the imidazole and carbonyl complexes. Oxidation and spin state marker bands of the undecapeptides are consistent with a six-coordinate, low spin iron in both oxidation states. Porphyrin core size correlations yield a porphyrin-centre to pyrrole-nitrogen distance of 2.00 A for MP11, suggestive of a six-coordinate species in a distorted heme environment. Molecular dynamics results show that the non-planarity of the heme of the parent cytochrome is conserved in the microperoxidase and its carbonmonoxy analog.

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“…21 Resonance Raman measurements of porphyrin core marker bands by Kostìc and co-workers, however, suggest that the porphyrin core is not sufficiently expanded in ZnCytc to permit an orthodox six-coordinate configuration. 22 The same group accounts for their finding that the Marcus reorganization energy for electron self-exchange between ZnCytc and ZnCytc + is lower than that obtained for the Fe(II) species by suggesting that Met 80 does not act as an axial ligand to the Zn(II) ion. 45 Having considered all of these results, we conclude that it is probable that the ligand coordination sphere for the Zn(II) ion in ZnCytc is six-coordinate, as imposed by the essentially native structure of the cytochrome c polypeptide.…”

Section: Discussionmentioning

confidence: 98%

Excited-State Axial-Ligand Photodissociation and Nonpolar Protein-Matrix Reorganization in Zn(II)-Substituted Cytochromec

2004

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We have obtained picosecond time-resolved fluorescence spectra from Zn(II)-substituted cytochrome c (ZnCytc) over the 100-ps to 12-ns time scale. The vibronic structure of the Q-band fluorescence spectrum exhibits a pronounced biexponential response (τ 1 ) 120 ps, τ 2 ) 7 ns), with the 0-0 band decreasing and the 0-1 band increasing in intensity in a mirror-image fashion with respect to time. These changes evidence a sequential photodissociation of the Zn(II) ion's two axial ligands, which are likely to be supplied by the side chains of the Met 80 and His 18 residues, as in the Fe(II,III)-containing molecule. The time constant for the fast phase of response is significantly slowed when the external solvent contains 50% (v/v) glycerol. These results show that the breaking of the first axial-ligand bond is rate limited by the reorganization of the surrounding protein matrix, which in turn is damped by the surrounding solvent. The protein-matrix response to the axial-ligand photodissociation reaction in ZnCytc is an example of nonpolar solvation dynamics, a reorganization of the protein structure in response to a change in size of an imbedded structure.

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Characterization of zinc-substituted cytochrome c by circular dichroism and resonance Raman spectroscopic methods

Cited by 44 publications

References 68 publications

Binding Specificity of the Porphyromonas gingivalis Heme and Hemoglobin Receptor HmuR, Gingipain K, and Gingipain R1 for Heme, Porphyrins, and Metalloporphyrins

Binding Specificity of the Porphyromonas gingivalis Heme and Hemoglobin Receptor HmuR, Gingipain K, and Gingipain R1 for Heme, Porphyrins, and Metalloporphyrins

Microperoxidase-11: Molecular Dynamics and Q-Band Excited Resonance Raman of the Oxidized, Reduced and Carbonyl Forms

Excited-State Axial-Ligand Photodissociation and Nonpolar Protein-Matrix Reorganization in Zn(II)-Substituted Cytochromec

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