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Oxidative phosphorylation

Structure of complex

Structure of complex erervert Matrix (Nn side) Succinate Fumarate NADH + H® Proton-mative force me i ie | ae FIGURE 19-19 Chemiosmotic model. In this simple representation of the and an electrical gradient (Ay) (combined, the proton-motive forc: 779 chemiosmotic theory applied to mitochondria, electrons from NADH and inner mitochondrial membrane is impermeable to protons; protons other oxidizable substrates pass through a chain of carriers arranged asym= reenter the matrix only through proton-specific channels ¢F,). The proton metrically in the inner membrane. Electron flow is accompanied by proton motive force that drives protons back into the matrix provides the energy for transfer across the membrane, producing both a chemical gradient (ApH) ATP synthesis, catalyzed by the F, complex associated with F, FIGURE 19-25 Mitochondrial ATP synthase complex. Ca? A Cartoon view et the fof) camplos €63 CPD 1D TRME and PISS 1D TINWZ Fy viewed troon Bhave (that in. trom the N side of the mmmbrane), showing the three / Cehades of purple? and three « Cehades of gray? subunits and the central shalt Cy subunit, green. acl suburnl, ear rls wlan face weithy her sci Goreng subunit hes a nucleotide binding site cntical to the colalyle ae fivity The single 7 subunit aecaciates primarily with one of the thran oft Rates, forcing each of the three ff subunits into slightly aitfarant cantarma- ene Subumt GF ADP? has ADP Cyellow) wi its Lindam, site, the rent Cs ATP) has ATP Ged? and Une third GS ernply? has no bound tueleotele Ce) The entire enzyme viewed frore thie sie Gin the plane of the caer tien (PDB Ie TOME, UNM, and 2AZU> nas thres @ and have beer anering) of identical © subunits, small, hydrophobic proteins The ering and subunit has an Acp residue neur the eniddle of Une trernbrane, which car ruclure ¢POS ID TYCE>, we have olor ATPase of ftyobecter lurtares, lor Whei bound Ma! lone Cred opheres>. €82 A view of Fy perpericicaian bo Ure rrembrane. Each of Ute © subunits 1 Fo hes ¢ crbeal Ase residue near the fiddle ef Use mennibrare, which undences protonalion/duprateriatesrr ducing the catalytic cycle of the ATP ayathace Asin Co) red spheres repre b> Tep view of Fy Bottom view of F, 19.2 ATP Sunthesis 753 7s4 Oxidative Phosphorylation and Photophespnorylation FIGURE 19-26 Ginding-change model fer ATP synthase. THe 6) complex has theese Renequivelont adenine nucicotide-cincing sites, ona for cach pair ofa ana ef sucunies. Bahay given mament, one of thease sites team the ff ATP comfermanion Chen Binds INTE tamtly>, o second iin the SADE Cloose-bindima> confermaten, and = third ite DPECUGCLIGE: O1 Liis: Redenetiease—eBeannsce: Reeqanad ts, aebeeraledwxesttanben Se cevewes: ©3Re ees is synthesizing ATP and in the omposita direction witer Une croeyine is Bevetrolysins: “rr Pbis prediction of rotation with ATE hydrolysis was com fowaecd im clogant oxperiments in the Isborateries of Masnsuie Yoshida and Kasuhilee Kingsita, Ir. Phe rec ion OF Y in u sinsde I, rmoiecule wis Observed micro ectogaiecalige Fas sattzaesPiieaas Vesrtat, bates, Claacomessceserett saectire wo —use>. polyiter Loy arch wotcbise At nuove: rudutive: to cng. ter Souetine witie ti Hiutebiibecd ta: a salcrosecpse: wide: ts Acid waass duel poerees iyaed. Cite csusccted reversal of the rotation wher ATE In oalzgs upattrussiaed cole: acl ber beuteed in Le Bhat ment, here is no proton gradient to arive Are ite mein Bis) Swnen the entire ©e, sommes (nee just — 7EBs5 and fhe Gsca in a similar cuparinant, ene ontirea ring Of < Manus one conmplate rata Unies torte with SGI. FS L2 75. Phe sahatee rerrened i eyere ONG prcaicltod Gircetiog: URroUsht GO". lhe rotation: was Sua Fox hoe Soon. but occurred in three discrete stapes of 120°. a —— = nase rea — aes lowered from 2 to 4: Psolat estes trams ved prvibesesbrcorvede ics Lo iptecesbocttercd