Literature DB >> 169914

The effect of temperature on the spectroscopic properties of the heme c octapeptide from cytochrome c.

G C Wagner, R J Kassner.   

Abstract

The effect of temperature on the optical properties of the acetylated heme c octapeptide from cytochrome c was examined. At above ambient temperatures the observed optical spectrum with maxima at 549 and 424 nm was characteristic of high-spin ferrous hemeproteins. At below ambient temperatures the optical spectrum became characteristic of low-spin ferrous hemeproteins with maxima at 547, 518, and 410 nm. A thermodynamic characterization of this two component system yielded a deltaHO of -10.1 +/- 0.7 kcal/mol and a delta S0 of-37.6 +/- 2.5 e.u. for the temperature dependent process. Discussion of the spectroscopic and thermodynamic parameters was presented in terms of the consistent magnetic and structural properties of heme complexes.

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Year:  1975        PMID: 169914     DOI: 10.1016/0005-2795(75)90331-1

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  1 in total

1.  Magnetic circular dichroism studies of myoglobin, hemoglobin and peroxidase at room and low temperatures. Ferrous high spin derivatives.

Authors:  Y A Sharonov; A P Mineyev; M A Livshitz; N A Sharonova; V B Zhurkin; Y P Lysov
Journal:  Biophys Struct Mech       Date:  1978-04-13
  1 in total

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