{"id":265740,"date":"2026-07-16T14:24:04","date_gmt":"2026-07-16T11:24:04","guid":{"rendered":"https:\/\/1kitap1.com\/en\/lehninger-principles-of-biochemistry-8th-edition-david-l-nelson-and-michael-m-cox\/"},"modified":"2026-07-16T14:24:04","modified_gmt":"2026-07-16T11:24:04","slug":"lehninger-principles-of-biochemistry-8th-edition-david-l-nelson-and-michael-m-cox","status":"publish","type":"post","link":"https:\/\/1kitap1.com\/en\/lehninger-principles-of-biochemistry-8th-edition-david-l-nelson-and-michael-m-cox\/","title":{"rendered":"Lehninger Principles Of Biochemistry 8th Edition – David L Nelson And Michael M Cox"},"content":{"rendered":"
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(a) In each pass through this four-step sequence, one acetyl residue (shaded in light red) is removed in the form of acetyl-CoA from the carboxyl end of the fatty acyl chain \u2014 in this example palmitate (C16), which enters as palmitoyl-CoA. Electrons from the first oxidation pass through electron transfer flavoprotein (ETF), and then through a second flavoprotein (ETF:ubiquinone oxidoreductase), into the respiratory chain.<\/p>\n

Electrons from the second oxidation enter the respiratory chain through NADH dehydrogenase. (b) Six more passes through the \u03b2- oxidation pathway yield seven more molecules of acetyl-CoA, the seventh arising from the last two carbon atoms of the 16-carbon chain. Eight molecules of acetyl-CoA are formed in all. The acetyl-CoA may be oxidized in the citric acid cycle, donating more electrons to the respiratory chain.<\/p>\n

This \ufb01rst step is catalyzed by three isozymes of acyl-CoA dehydrogenase, each speci\ufb01c for a range of fatty-acyl chain lengths: very-long-chain acyl-CoA dehydrogenase (VLCAD), acting on fatty acids of 12 to 18 carbons; medium-chain (MCAD), acting on fatty acids of 4 to 14 carbons; and short-chain (SCAD), acting on fatty acids of 4 to 8 carbons. VLCAD is in the inner mitochondrial membrane; MCAD and SCAD are in the matrix.<\/p>\n

All three isozymes are \ufb02avoproteins with tightly bound FAD (see Fig. 13-27) as a prosthetic group. The electrons removed from the fatty acyl\u2013CoA are transferred to FAD, and the reduced form of the dehydrogenase immediately donates its electrons to an electron carrier, the electron transfer \ufb02avoprotein (ETF) (see Fig.<\/p>\n

19-15). Electrons move from ETF to a second \ufb02avoprotein, ETF:ubiquinone oxidoreductase, and through ubiquinone into the mitochondrial respiratory chain. The oxidation catalyzed by an acyl-CoA dehydrogenase is analogous to succinate dehydrogenation in the citric acid cycle (p. 586); in both reactions the enzyme is bound to the inner membrane, a double bond is introduced into a carboxylic acid between the \u03b1 and \u03b2 carbons, FAD is the electron acceptor, and electrons from the reaction ultimately enter the respiratory chain and pass to O2, with the concomitant synthesis of about 1.5 ATP molecules per electron pair.<\/p>\n

In the second step of the \u03b2-oxidation cycle (Fig. 17-8a), water is added to the double bond of the trans-\u03942-enoyl-CoA to form the L stereoisomer of \u03b2-hydroxyacyl-CoA (3-hydroxyacyl-CoA). This reaction, catalyzed by enoyl-CoA hydratase, is formally analogous to the fumarase reaction in the citric acid cycle, in which H2O adds across an \u03b1\u2013\u03b2 double bond (p. 587). In the third step, L-\u03b2-hydroxyacyl-CoA is dehydrogenated to form \u03b2-ketoacyl-CoA, by the action of \u03b2-hydroxyacyl-CoA dehydrogenase; NAD+ is the electron acceptor. This enzyme is absolutely speci\ufb01c for the L stereoisomer of hydroxyacyl-CoA.<\/p>\n

The NADH formed in the reaction donates its electrons to NADH dehydrogenase (Complex I), an electron carrier of the respiratory chain (see Fig. 19-15), and ATP is formed from ADP as the electrons pass to O2.<\/p>\n

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H. Freeman and Company All rights reserved. 1 2 3 4 5 6 25 24 23 22 21 20 Macmillan Learning One New York Plaza Suite 4600 New York, NY 10004-1562 www.macmillanlearning.com 7 In 1946, William Freeman founded W. H. Freeman and Company and published Linus Pauling\u2019s General Chemistry, which revolutionized the chemistry curriculum and established the prototype for a Freeman text.<\/p>\n

W. H. Freeman quickly became a publishing house where leading researchers can make significant contributions to mathematics and science. In 1996, W. H. Freeman joined Macmillan and we have since proudly continued the legacy of providing revolutionary, quality educational tools for teaching and learning in STEM. 8 To Our Teachers Paul R. Burton Albert Finholt Jeff Gelles William P. Jencks Eugene P. Kennedy Homer Knoss Arthur Kornberg I. Robert Lehman Andy LiWang Patti LiWang Melissa J.<\/p>\n

Moore Douglas A. Nelson Wesley A. Pearson David E. Sheppard JoAnne Stubbe Harold B. White 9 About the Authors David L. Nelson, born in Fairmont, Minnesota, received his BS in chemistry and biology from St. Olaf College in 1964, and earned his PhD in biochemistry at Stanford Medical School, under Arthur Kornberg. He was a postdoctoral fellow at the Harvard Medical School with Eugene P. Kennedy, who was one of Albert Lehninger\u2019s \ufb01rst graduate students.<\/p>\n

Nelson joined the faculty of the University of Wisconsin\u2013Madison in 1971 and became a full professor of biochemistry in 1982. For eight years he was Director of the Center for Biology Education at the University of Wisconsin\u2013Madison.<\/p>\n<\/blockquote>\n

This is a short excerpt from the opening of “” by Unknown, quoted for review and introduction purposes. All rights belong to the copyright holders.<\/em><\/p>\n

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