Modification of histidine 56 in adrenodoxin with diethyl pyrocarbonate inhibited the interaction with cytochrome P-450scc and adrenodoxin reductase.

Miura, Shigetoshi; Tomita, Shuhei; Ichikawa, Yoshiyuki

doi:10.1016/s0021-9258(18)54984-x

Cited by 23 publications

(17 citation statements)

References 30 publications

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“…Thus, its pXa value must be below 5. These results are consistent with those of Miura et al (1991), which showed that His56 of oxidized bovine ferredoxin does not exhibit a normal histidine titration curve. They attributed this to an interaction between His56 and Ser88.…”

Section: Effects Of Phsupporting

confidence: 92%

“…The pKa for His10 is 6.45 and that of His62 is 5.78; both values are lower than the histidine pKa value (6.9) reported from the study of a model peptide (Markley, 1975). They are also lower than the pXa values reported for bovine ferredoxin: 6.61 and 6.12 in Greenfield et al (1989); 6.6 and 6.0 in Miura et al (1991).…”

Section: Effects Of Phcontrasting

confidence: 60%

“…The peak that Greenfield et al (1989) assigned to the 61 of His56 of oxidized bovine ferredoxin corresponds to the small peak near 7.80 ppm between the two *Hel peaks of His10 and His62 in the ID NMR spectrum of human ferredoxin (Figure 2). In subsequent studies, Ichikawa and co-workers assigned a peak at 7.52 ppm to ' € and one at 7.05 ppm to 52 of His56; these assignments were supported by data from the chemical modification of the histidine with DEP (Miura & Ichikawa, 1991b;Miura et al, 1991). The latter assignments are consistent with the present results with human ferredoxin.2 In the present study, spectral overlaps in the spectrum of human ferredoxin necessitated the use of 15N and 13C labeling and multinuclear NMR methods in order to identify the His56 spin system unambiguously; these provided complete side-chain , 13C, and 15N assignments.…”

Section: Discussionmentioning

confidence: 84%

“…Histidine 56, which is adjacent to one of the iron-sulfur cluster ligand cysteines (Cys55) and is conserved in all vertebrate ferredoxins (Figure 1), is the most interesting of the three histidines of human ferredoxin. Previous studies suggested that His56 plays an important role in binding with ferredoxin reductase and cytochrome P450scc (Miura & Ichikawa, 1991b;Miura et al, 1991). It also was suggested that His56 is responsible for the pH dependence of the reduction potential of the iron-sulfur cluster (Lambeth et al, 1982;Greenfield et al, 1989).…”

Section: Discussionmentioning

confidence: 99%

“…Subsequently, Miura and Ichikawa (1991a) assigned signals from two of the histidines specifically to His10 and His62 by comparing the ID and 2D NMR spectra of bovine ferredoxin with the spectra of ovine ferredoxin, which lacks His10. However, they proposed a different assignment for His56 (Miura & Ichikawa, 1991b;Miura et al, 1991). The paramagnetically shifted (hyperfine) signals of several vertebrate ferredoxins (including human and bovine) also have been reported (Skjeldal et al, 1991), but these studies did not reveal any signals that could be assigned to a histidine residue interacting with the ironsulfur cluster.…”

mentioning

confidence: 98%

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Multinuclear Magnetic Resonance and Mutagenesis Studies of the Histidine Residues of Human Mitochondrial Ferredoxin

Xia¹,

Cheng²,

Skjeldal³

et al. 1995

Biochemistry

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Human mitochondrial ferredoxin is a [2Fe-2S] protein that functions to transfer electrons from NADPH-dependent ferredoxin reductase to cytochrome P450 enzymes. Two of the three histidines of human ferredoxin are strictly conserved in the sequences of all known vertebrate ferredoxins, and one of these (His56) is adjacent to Cys55, which serves as one of the ligands to the iron-sulfur cluster. All but 16 of its residues show sequence identity with those of bovine ferredoxin. It has been proposed for bovine ferredoxin that His56 hydrogen bonds with a labile sulfur and that the reduction of the iron-sulfur center is accompanied by the uptake of a proton by this histidine [Lambeth, J. D., Seybert, D. W., Lancaster, J. R., Jr., Salerno, J. C., & Kamin, H. (1982) Mol. Cell. Biochem. 45, 13-31]. In this paper, we report procedures for labeling human ferredoxin uniformly with 15N using 15NH4Cl and selectively with 13C by the incorporation of [U-13C]histidine. Most of the imidazole 1H, 13C, and 15N resonances of the three histidines have been assigned by heteronuclear two-dimensional single- and multiple-bond correlation spectroscopy. Site-directed mutagenesis was used in assigning the NMR signals from His56. The pKa values of His10 (6.5) and His62 (5.8) in oxidized human ferredoxin were found to be similar to those reported previously for the corresponding residues of bovine ferredoxin [Greenfield, N. J., Wu, X., & Jordan, F. (1989) Biochim. Biophys. Acta 995, 246-254; Miura, S., Tamita, S., & Ichikawa, Y. (1991) J. Biol. Chem. 266, 19212-19216].(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Effects Of Phsupporting

confidence: 92%

Section: Effects Of Phcontrasting

confidence: 60%

Section: Discussionmentioning

confidence: 84%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 98%

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Multinuclear Magnetic Resonance and Mutagenesis Studies of the Histidine Residues of Human Mitochondrial Ferredoxin

Xia¹,

Cheng²,

Skjeldal³

et al. 1995

Biochemistry

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Adrenodoxin: Structure, stability, and electron transfer properties

et al. 2000

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Adrenodoxin is an iron‐sulfur protein that belongs to the broad family of the [2Fe‐2S]‐type ferredoxins found in plants, animals and bacteria. Its primary function as a soluble electron carrier between the NADPH‐dependent adrenodoxin reductase and several cytochromes P450 makes it an irreplaceable component of the steroid hormones biosynthesis in the adrenal mitochondria of vertebrates. This review intends to summarize current knowledge about structure, function, and biochemical behavior of this electron transferring protein. We discuss the recently solved first crystal structure of the vertebrate‐type ferredoxin, the truncated adrenodoxin Adx(4‐108), that offers the unique opportunity for better understanding of the structure‐function relationships and stabilization of this protein, as well as of the molecular architecture of [2Fe‐2S] ferredoxins in general. The aim of this review is also to discuss molecular requirements for the formation of the electron transfer complex. Essential comparison between bacterial putidaredoxin and mammalian adrenodoxin will be provided. These proteins have similar tertiary structure, but show remarkable specificity for interactions only with their own cognate cytochrome P450. The discussion will be largely centered on the protein‐protein recognition and kinetics of adrenodoxin dependent reactions. Proteins 2000;40:590–612. © 2000 Wiley‐Liss, Inc.

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Redox‐dependent dynamics of putidaredoxin characterized by amide proton exchange

Lyons¹,

Ratnaswamy²,

Pochapsky³

1996

Protein Science

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Multidimensional NMR methods were used to obtain 'H-I'N correlations and "N resonance assignments for amide and side-chain nitrogens of oxidized and reduced putidaredoxin (Pdx), the Fe2S2 ferredoxin, which acts as the physiological reductant of cytochrome P-450,,, (CYPlOl). A model for the solution structure of oxidized Pdx has been determined recently using NMR methods (Pochapsky TC, Ye XM, Ratnaswamy G, Lyons TA, 1994, Biochemistry 33:6424-6432) and redox-dependent ' H NMR spectral features have been described (Pochapsky TC, Ratnaswamy G, Patera A, 1994, Biochemistry33:6433-6441). "N assignments were made with NOESY-('H/''N) HMQC and TOCSY-('H/''N) HSQC spectra obtained using samples of Pdx uniformly labeled with "N. Local dynamics in both oxidation states of Pdx were then characterized by comparison of residue-specific amide proton exchange rates, which were measured by a combination of saturation transfer and H 2 0 / D 2 0 exchange methods at pH 6.4 and 7.4 (uncorrected for isotope effects). In general, where exchange rates for a given site exhibit significant oxidation-state dependence, the oxidized protein exchanges more rapidly than the reduced protein. The largest dependence of exchange rate upon oxidation state is found for residues near the metal center and in a region of compact structure that includes the loop-turn Val 74-Ser 82 and the C-terminal residues (Pro 102-Trp 106). The significance of these findings is discussed in light of the considerable dependence of the binding interaction between Pdx and CYPlOl upon the oxidation state of Pdx.

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Modification of histidine 56 in adrenodoxin with diethyl pyrocarbonate inhibited the interaction with cytochrome P-450scc and adrenodoxin reductase.

Cited by 23 publications

References 30 publications

Multinuclear Magnetic Resonance and Mutagenesis Studies of the Histidine Residues of Human Mitochondrial Ferredoxin

Multinuclear Magnetic Resonance and Mutagenesis Studies of the Histidine Residues of Human Mitochondrial Ferredoxin

Adrenodoxin: Structure, stability, and electron transfer properties

Redox‐dependent dynamics of putidaredoxin characterized by amide proton exchange

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