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Myoglobin 4-state model

Slower processes occurring in the /as time scale were also studied by flash photolysis. Interpretation of the kinetic data requires a four-state model shown in equation (4) where MbL represents myoglobin with the small ligand bound at six-coordinated Fe(II), Mb L (generated by photodissociation) represents the short-lived... [Pg.221]

Table 3.4 lists values for A Eq and for some important oxidation and spin states found in bioinorganic molecules. Data are taken from reference 24 and from Table 1 of reference 25 for hemoglobin, myoglobin, and the picket-fence porphyrin model compound, FeTpivPP(l-Melm).25 The myoglobin and hemoglobin model compounds are discussed in Section 4.8.2. Reference 26 provides the Table 3.4 data on iron sulfur clusters found in many bioinorganic species.26 The unusual iron-sulfur and iron-molybdenum-sulfur clusters found in the enzyme nitrogenase are discussed more fully below and in Chapter 6. [Pg.117]

The dioxygen-carrying proteins, hemoglobin and myoglobin, as well as the many synthetic model systems that have been developed recently,44 will not be considered here in this chapter since their chemistry is mainly that of iron in the + 2 oxidation state. The present chapter is therefore restricted to a brief description of the structure and reactivity of some cytochrome and peroxidase proteins. [Pg.263]

Spectroscopic data obtained from spectroelectrochemical experiments require careful and case-specific analysis. The Fe /Fe redox couple has a unique role in diflferent iron-containing proteins. It is hypothesised that the mammalian iron-transport protein transferrin uses the Fe /Fe redox couple as a switch that controls the time and site-specific release of iron, while other iron-containing proteins, such as myoglobin, are able to hold on to iron in both oxidation states. Therefore, it is very important to evaluate the protein and its interaction with both the oxidised and reduced states of iron and accordingly develop a data-analysis model. The spectroelectrochemical response of an iron binding protein can be ideal Nernstian, non-Nernstian resulting from coupled... [Pg.38]


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