Semisynthetic horse heart [65-homoserine]cytochrome
            <i>c</i>
            from three fragments

Boon, P.J.; Tesser, G. I.; Nivard, R. J. F.

doi:10.1073/pnas.76.1.61

Cited by 24 publications

(10 citation statements)

References 14 publications

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“…In order to avoid the undesirable presence of material denatured by freeze-drying from acidic solutions (Boon et al, 1978), we treated each freeze-dried product with phosphate/urea buffer followed by gel filtration according to the method of Boon et al (1979). We adjusted the buffer to pH 8.0 and included 0.1 M-borate to stabilize the DHCH adduct.…”

Section: Introductionmentioning

confidence: 99%

The oxidation-state-dependent ATP-binding site of cytochrome c. Implication of an essential arginine residue and the effect of occupancy on the oxidation-reduction potential

Corthésy¹,

Wallace²

1988

Biochemical Journal

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Arg-91 is not part of the active site of cytochrome c that mediates binding and electron transfer, yet it is absolutely conserved in eukaryotic cytochromes c, indicating a special function. The physicochemical properties of analogues are unaffected by the modification of this residue, so they can be used with confidence to study the role of Arg-91. We have established limiting conditions under which this residue alone is specifically modified by cyclohexane-1,2-dione, and have subsequently shown that ATP, and to a lesser extent ADP or P1, protects it from the action of the reagent in an oxidation-state-dependent manner. These observations strongly support the idea that this site exerts a controlling influence on cytochrome c activity in the electron transport or other cellular redox systems, and we have commenced a study of how that influence might operate. We find that the redox potentials of both cytochrome c and analogue are little affected by changing ATP or Pi concentrations.

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Section: Introductionmentioning

confidence: 99%

The oxidation-state-dependent ATP-binding site of cytochrome c. Implication of an essential arginine residue and the effect of occupancy on the oxidation-reduction potential

Corthésy¹,

Wallace²

1988

Biochemical Journal

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“…6). There are small differences: in the Eadie-Hofstee plots, native cytochrome c and its HseO analogue (6) are represented by the curve with the greatest slope. The substitution at position 67 causes-as found before (18)-a higher reaction rate, but the smaller slope points to a greater Michaelis constant.…”

Section: Resultsmentioning

confidence: 99%

“…The same reasoning led to the exchange Thr78 -+ Val. The analogues would be accessible by using the available strategy (6).…”

Section: Resultsmentioning

confidence: 99%

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Semisynthesis of horse heart cytochrome c analogues from two or three fragments.

Kortenaar¹,

Adams²,

Tesser³

1985

Proc. Natl. Acad. Sci. U.S.A.

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“…Coupling reactions were performed in 0.1 M NaAc, pH 5.7, with peptide and protein concentrations in the millimolar range to promote complexation of protein and hormone fragments when possible. Formation of noncovalent complexes by fragments was assumed to promote coupling efficiency as shown by previous experiments with cytochrome c (Corradin and Harbury, 1971;Boon et al, 1979;Ten Kortenaar et al, 1985), RNase A (Sheppard, 1979) and pancreatic trypsin inhibitor (Sheppard, 1979). Incorporation of ''C-acetimidyl groups in the vasopressinyl peptides made it easier to follow the semisynthesis reaction and identify the products (Fig.…”

Section: Semisynthesis Of Proavp/npii Precursor and Avp Domain-redesimentioning

confidence: 94%

Sequence simplification and the intra‐ and intermolecular self‐recognition properties of vasopressin/neurophysin biosynthetic precursor

Fassina

Chaiken

1989

J of Molecular Recognition

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The self-assembly properties of the arginine 8-vasopressin/bovine neurophysin II (AVP/BNPII) biosynthetic precursor were studied using glycopeptide-deleted and sequence-redesigned semisynthetic derivatives. Semisynthetic precursors were prepared by chemically coupling synthetic vasopressinyl sequence domains and native protein-derived neurophysin II domain. Measurement of precursor-protein association by the extent of affinity chromatographic retardation on agarose-immobilized BNPII verified that the semisynthetic precursor with native AVP sequence has an enhanced self-association propensity similar to that predicted for native precursor. Here, the stabilizing contacts between hormone and neurophysin domains, mainly the positively charged protonated alpha-amino group and tyrosyl 2 side chain of the hormone, are retained. Semisynthetic precursor variants in which the hormone domain is sequence-simplified by introducing alanyl residues in positions not considered important for neurophysin recognition show non-reduced association to BNPII. In contrast, removal of one of the main contact elements between hormone and neurophysin by acetylation of the hormone alpha-amino group abolishes potentiation of precursor self-association. The results show that the presence of the C-terminal glycopeptide sequence domain of native vasopressin precursor is not required to promote self-assembly of the precursor. The data verify the view proposed for the oxytocinyl precursor that intramolecular domain interaction is the triggering event which promotes the increase in affinity of precursor self-association (intermolecular self-recognition). The data also define some of the intramolecular self-recognition elements in the folded precursor required for the high affinity intermolecular self-recognition.

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Semisynthetic horse heart [65-homoserine]cytochrome c from three fragments

Abstract: Horse heart cytochrome c was treated with methylsulfonylethyloxycarbonyl succinimide (Msc-ONSu)

Cited by 24 publications

References 14 publications

The oxidation-state-dependent ATP-binding site of cytochrome c. Implication of an essential arginine residue and the effect of occupancy on the oxidation-reduction potential

The oxidation-state-dependent ATP-binding site of cytochrome c. Implication of an essential arginine residue and the effect of occupancy on the oxidation-reduction potential

Semisynthesis of horse heart cytochrome c analogues from two or three fragments.

Sequence simplification and the intra‐ and intermolecular self‐recognition properties of vasopressin/neurophysin biosynthetic precursor

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