1 to 6 of 6 literature results

• An EPR study of the dinuclear iron site in the soluble methane monooxygenase from Methylococcus capsulatus (Bath) reduced by one electron at 77 K: the effects of component interactions and the binding of small molecules to the diiron(III) center.

  Reduction of the soluble methane monooxygenase hydroxylase (MMOH) from Methylococcus capsulatus (Bath) in frozen 4:1 buffer/glycerol solutions at 77 K…

  Authors: R Davydov, A M Valentine, S Komar-Panicucci, B M Hoffman, S J Lippard

  Source: Biochemistry. 1999 Mar 30

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• Modulated growth of Saccharomyces cerevisiae by altering the driving force of the reactions of cytochrome c: Marcus' theory in vitro and in vivo.

  According to Marcus' theory, rates of electron transfer reactions depend parabolically on the free energy of reaction. Amino acid replacements in the …

  Authors: S Komar-Panicucci, F Sherman, G McLendon

  Source: Biochemistry. 1996 Apr 16

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• Structural and functional effects of multiple mutations at distal sites in cytochrome c.

  Multiple mutations at distally located sites have been introduced into yeast iso-1 cytochrome c to determine the contributions of three amino acids to…

  Authors: T P Lo, S Komar-Panicucci, F Sherman, G McLendon, G D Brayer

  Source: Biochemistry. 1995 Apr 18

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• Thermodynamics of the equilibrium unfolding of oxidized and reduced Saccharomyces cerevisiae iso-1-cytochromes c.

  We report thermodynamic data for the chemical denaturation of iso-1-cytochromes c from Saccharomyces cerevisiae having amino acid substitutions R38A, …

  Authors: S Komar-Panicucci, D Weis, G Bakker, T Qiao, F Sherman, G McLendon

  Source: Biochemistry. 1994 Aug 30

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• Strand-specificity in the transformation of yeast with synthetic oligonucleotides.

  Cyc1 mutants of the yeast Saccharomyces cerevisiae were directly transformed with both sense and antisense oligonucleotides to examine the involvement…

  Authors: T Yamamoto, R P Moerschell, L P Wakem, S Komar-Panicucci, F Sherman

  Source: Genetics. 1992 Aug

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• Electron transfer in cytochrome c depends upon the structure of the intervening medium.

  BACKGROUND: Long-distance electron-transfer (ET) reactions through proteins are involved in a great many biochemical processes; however, the way in wh…

  Authors: T B Karpishin, M W Grinstaff, S Komar-Panicucci, G McLendon, H B Gray

  Source: Structure (London, England : 1993). 1994 May 15

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