Review terms and
definitions Focus your studying with a path Get faster at matching terms - Both globins and cytochromes
are hemoproteins, but with contrasting functions. In globins such as myoglobin and hemoglobin, the heme group functions to store and carry oxygen, so the heme binds and release O2. In cytochromes, the heme group functions to transfer electrons. Recommended textbook solutions
 How do cytochromes differ from hemoglobin?No, haemoglobin is not a cytochrome. The main function of cytochromes is redox catalysis, wherein the iron found in the heme core is interconverted between Fe(II) and Fe(III) state. The main function of haemoglobin is to bind and transport oxygen. In the Ferric state (FeIII), it cannot combine with oxygen.
What unusual property do cytochromes have in common with hemoglobin or myoglobin quizlet?What unusual property do cytochromes have in common with hemoglobin or myoglobin? All of them contain heme groups.
What are cytochromes and what is their role in this process?Cytochromes are redox-active proteins containing a heme, with a central Fe atom at its core, as a cofactor. They are involved in electron transport chain and redox catalysis.
What accounts for this difference in iron oxidation states between hemoglobin and cytochromes?The cytochromes are designed to "hold and pass" electrons, so they are built to engage in 'normal' operations--the ability for the iron to have an electron (Fe2+) or lose it (Fe3+) depending on what other molecule is present to 'take' or 'donate' an electron. Hemoglobin is precisely designed NOT to permit this.
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How do cytochromes differ from hemoglobin and myoglobin in terms of chemical activity quizlet?
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