Solution Structure of Oxidized Saccharomyces cerevisiae Iso-1-cytochrome c,

Banci, Lucia; Bertini, Ivano; Bren, Kara L.; Gray, Harry B.; Sompornpisut, Pornthep; Turano, Paola

doi:10.1021/bi963025c

Cited by 121 publications

(186 citation statements)

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“…Moreover, both structures are, within the indetermination of the family, substantially similar to the corresponding X-ray structures (Baistrocchi et al, 1996;Banci et al, 1997a). The similarity is especially evident for the backbone conformation.…”

Section: Discussionsupporting

confidence: 65%

“…The results obtained for hh cyt c and for S. cereVisiae cytochrome c (Banci et al, 1997a) are shown in Table 3. They are somewhat different from those already reported (Gao et al, 1990;Turner, 1993) and sensibly different from those calculated from the 13 C data (Turner, 1995).…”

Section: Magnetic Susceptibility Tensormentioning

confidence: 99%

“…The standard deviation of the calculated pseudocontact shift is reported. The tensor parameters for S. cereVisiae cytochrome c have been taken from Banci et al (1997a). b The shifts of the reduced species are taken from Santos and Turner (1992).…”

Section: Structure Analysismentioning

confidence: 99%

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Solution Structure of Oxidized Horse Heart Cytochrome c^,

et al. 1997

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The solution structure of oxidized horse heart cytochrome c was obtained at pH 7.0 in 100 mM phosphate buffer from 2278 NOEs and 241 pseudocontact shift constraints. The final structure was refined through restrained energy minimization. A 35-member family, with RMSD values with respect to the average structure of 0.70 ( 0.11 Å and 1.21 ( 0.14 Å for the backbone and all heavy atoms, respectively, and with an average penalty function of 130 ( 4.0 kJ/mol and 84 ( 3.7 kJ/mol for NOE and pseudocontact shift constraints, respectively (corresponding to a target function of 0.9 Å 2 and 0.2 Å 2 ), was obtained. The solution structure is somewhat different from that recently reported (Qi et al., 1996) and appears to be similar to the X-ray structure of the same oxidation state (Bushnell et al., 1990). A noticeable difference is a rotation of 17 ( 8°of the imidazole plane between solid and solution structure. Detailed and accurate structural determinations are important within the frame of the current debate of the structural rearrangements occurring upon oxidation or reduction. From the obtained magnetic susceptibility tensor a separation of the hyperfine shifts into their contact and pseudocontact contributions is derived and compared to that of the analogous isoenzyme from S. cereVisiae and to previous results.

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Section: Discussionsupporting

confidence: 65%

Section: Magnetic Susceptibility Tensormentioning

confidence: 99%

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Solution Structure of Oxidized Horse Heart Cytochrome c^,

et al. 1997

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“…The two proteins have a similar tertiary architecture [14][15][16][17], but yeast cyt c displays a significantly lower stability than the protein from horse, it does not bind ATP and, contrary to horse cyt c, lacks pro-apoptotic activity [18,19]. The CL-cyt c binding reaction has been investigated in the absence and in the presence of ATP and sodium chloride, two compounds that significantly influence the (horse cyt c)-CL binding process [5].…”

Section: Introductionmentioning

confidence: 99%

The effects of ATP and sodium chloride on the cytochrome c–cardiolipin interaction: The contrasting behavior of the horse heart and yeast proteins

Sinibaldi¹,

Droghetti²,

Polticelli³

et al. 2011

Journal of Inorganic Biochemistry

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In cells a portion of cytochrome c (cyt c) (15-20%) is tightly bound to cardiolipin (CL), one of the phospholipids constituting the mitochondrial membrane. The CL-bound protein, which has nonnative tertiary structure, altered heme pocket, and disrupted Fe(III)-M80 axial bond, is thought to play a role in the apoptotic process. This has attracted considerable interest in order to clarify the mechanisms governing the cyt c-CL interaction. Herein we have investigated the binding reaction of CL with the c-type cytochromes from horse heart and yeast. Although the two proteins possess a similar tertiary architecture, yeast cyt c displays lower stability and, contrary to the equine protein, it does not bind ATP and lacks pro-apoptotic activity. The study has been performed in the absence and in the presence of ATP and NaCl, two compounds that influence the (horse cyt c)-CL binding process and, thus, the pro-apoptotic activity of the protein. The two proteins behave differently: while CL interaction with horse cyt c is strongly influenced by the two effectors, no effect is observed for yeast cyt c. It is noteworthy that NaCl induces dissociation of the (horse cyt c)-CL complex but has no influence on that of yeast cyt c. The differences found for the two proteins highlight that specific structural factors, such as the different local structure conformation of the regions involved in the interactions with either CL or ATP, can significantly affect the behavior of cyt c in its reaction with liposomes and the subsequent pro-apoptotic action of the protein.

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“…The system was studied with both proteins in the reduced state since it was impossible for us to keep one or both proteins in the oxidized state for the long time of the NMR experiments. The characterization of these adducts still has a biological meaning, as the surfaces and their electrostatic potentials are not affected by the redox state (as witnessed by the comparison of the structures in the two states [17,18,19,20]) and therefore are expected to provide relevant information about the adducts. 15 N chemical shifts were monitored through 1 H-15 N HSQC experiments, which are very sensitive and thus relatively quick.…”

Section: Introductionmentioning

confidence: 99%

A further investigation of the cytochrome b 5–cytochrome c complex

et al. 2003

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The interaction of reduced rabbit cytochrome b 5 with reduced yeast iso-1 cytochrome c has been studied through the analysis of 1 H-15 N HSQC spectra, of 15 N longitudinal (R 1 ) and transverse (R 2 ) relaxation rates, and of the solvent exchange rates of protein backbone amides. For the first time, the adduct has been investigated also from the cytochrome c side. The analysis of the NMR data was integrated with docking calculations. The result is that cytochrome b 5 has two negative patches capable of interacting with a single positive surface area of cytochrome c. At low protein concentrations and in equimolar mixture, two different 1:1 adducts are formed. At high concentration and/or with excess cytochrome c, a 2:1 adduct is formed. All the species are in fast exchange on the scale of differences in chemical shift. By comparison with literature data, it appears that the structure of one 1:1 adduct changes with the origin or primary sequence of cytochrome b 5 .

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Solution Structure of Oxidized Saccharomyces cerevisiae Iso-1-cytochrome c^,

Abstract: Proton assignments for the oxidized yeast iso-ferricytochrome c at 303 K Note: The underlined chemical shift values indicate the stereospecific assignments for disastereotopic pairs of methylene protons or isopropyl methyl groups.

Cited by 121 publications

References 50 publications

Solution Structure of Oxidized Horse Heart Cytochrome c^,

Solution Structure of Oxidized Horse Heart Cytochrome c^,

The effects of ATP and sodium chloride on the cytochrome c–cardiolipin interaction: The contrasting behavior of the horse heart and yeast proteins

A further investigation of the cytochrome b 5–cytochrome c complex

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Solution Structure of Oxidized Saccharomyces cerevisiae Iso-1-cytochrome c,

Abstract: Proton assignments for the oxidized yeast iso-ferricytochrome c at 303 K Note: The underlined chemical shift values indicate the stereospecific assignments for disastereotopic pairs of methylene protons or isopropyl methyl groups.

Cited by 121 publications

References 50 publications

Solution Structure of Oxidized Horse Heart Cytochrome c,

Solution Structure of Oxidized Horse Heart Cytochrome c,

The effects of ATP and sodium chloride on the cytochrome c–cardiolipin interaction: The contrasting behavior of the horse heart and yeast proteins

A further investigation of the cytochrome b 5–cytochrome c complex

Contact Info

Product

Resources

About

Solution Structure of Oxidized Saccharomyces cerevisiae Iso-1-cytochrome c^,

Solution Structure of Oxidized Horse Heart Cytochrome c^,

Solution Structure of Oxidized Horse Heart Cytochrome c^,