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Biochem Unit 2 > Ackerman Lectures 5-8 > Flashcards

Ackerman Lectures 5-8 Flashcards

1
Q

complex I

A

NADH dehydrogenase; NADH is donor, Q is acceptor; cofactors are FMN, FeS; OxPhos E coupling site 1; 4H+ pumped per 2e- transferred (-17kcal/mol)

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2
Q

complex II

A

succinate dehydrogenase; 4 su’s; succinate is donor, Q is acceptor; cofactors are FAD, FeS, b-type heme (-0.7kcal/mol)

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3
Q

complex III

A

cytochrome b-c1; 11 su’s; OxPhos E coupling site 2; QH2 is donor, cyto coxid is acceptor; cofactors are b and c hemes, Rieske FeS cluster; prots are cytochrome b and c1, Rieske iron-sulfur prot; 2H+ pumped per 2e- transferred, plus 2H+ dumped outside from quinol (-9.6kcal/mol)

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4
Q

complex IV

A

cytochrome c oxidase (COX); 13 su’s; OxPhos E coupling site 3; cyto cred is donor, O2 is acceptor; cofactors are a-type hemes and copper (CuA and CuB); 2H+ pumped per 2e- transferred plus 2H+ used inside to make H2O (-26kcal/mol)

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5
Q

complex V

A

ATP synthase

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6
Q

bound redox centers of the ETC

A

flavins, copper, FeS centers, heme

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7
Q

heme A

A

IV

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8
Q

heme B

A

II and III

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9
Q

heme C

A

III

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10
Q

flavins

A

accept 2e-, 2H or 1e-, 1H (all others are just one, not two)

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11
Q

ubiquinone/coenz Q (semiquinone, ubiquinol)

A

3 oxid states; carries 1 or 2 e-; carries both e- and protons; isoprenoid side chain

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12
Q

cytochrome c

A

peripheral prot att to IMS face of inner memb; heme C is coval liganded

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13
Q

entry paths into ETC

A

all flavo-prots; CoQ is common acceptor; in each path, flavin + Q

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14
Q

respiratory substrates

A

NADH, succinate, fatty acyl-CoA, glycerol-3-P (all release 2e- at once)

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15
Q

subst-level phos

A

high-E metabolites–>7.3kcal/mol free E when cleaved (1,3-BPG, PEP, succ-CoA, phosphocreatine)

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16
Q

oxid phos

A

employs O2 as final acceptor of e- and H+ from metab oxid rxns

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17
Q

FAD

A

complex II, G3PDH, FA-CoA DH; 2 or 1 e- and H+

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18
Q

FMNH2

A

complex I; 2 or 1 e- and H+

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19
Q

FeS centers

A

1e-; Complex I, II, or III (III=Rieske type w/2Cys, 2His)

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20
Q

Heme A

A

1e-; complex IV

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21
Q

Heme B

A

1e-; complex II and III

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22
Q

Heme C

A

1e-; complex III; w/Cys sulfhydryls att

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23
Q

copper

A

1e-; complex IV

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24
Q

complex I rxn

A

NADH + H+ –> FMN; FMNH2–>(FeS)9 –> CoQ; must rel 2 e- at once

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25
Q

complex II rxn

A

succinate –> FAD; FADH2–>(FeS)3–>Cyt b –> CoQ; must rel 2 e- at once

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26
Q

NADH shuttle (G3PDH)

A

G3P–>FAD; FADH2–>CoQ; must rel 2 e- at once

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27
Q

b-oxid path (FA-CoADH)

A

FA-CoA –>FAD; FADH2–>CoQ; must rel 2 e- at once

28
Q

NADH as substrate

A

IMS: matrix is 10 per 2e- transferred (pmf=10)

29
Q

SUC or FA-CoA or Gly3P as substrate

A

IMS: matrix is 6 per 2e- transferred (pmf =6)

30
Q

respiration proton gradient

A

chem (pH) and charge gradients w/IMS more positive than matrix; contrib to change in free E as pmf (excess protons in IMS)

31
Q

ATP synthase

A

transducer that captures pmf E and converts it to chem bond E (1mol ATP made for every 4H+ translocated from IMS back to matrix); pmf (electrochem E) converted to rotation (mech E); E conserved in b-y phosphodiester (anhydride) bond b/w ADP and Pi

32
Q

F1

A

peripheral memb prot catalytic sites (3); a3b3y3e

33
Q

F0

A

integral memb prot proton channel; d+ab2c10

34
Q

catalytic head of ATP synthase

A

a3b3; catalytic site in each of 3 b subunits interfaces

35
Q

proton pump of ATP synthase

A

a(c ring); H+ transloc causes to rotate

36
Q

ATP synthase rotor

A

ye; att to c ring; rotate in unison

37
Q

ATP synthase stator

A

b2d + d; prevents rotation of a3b3 head gp

38
Q

Keq of ATP hydrolysis

A

1; cat coop b/w 3 sites; freely reversible; ATP+H2O–>ADP+Pi and ADP+Pi–>ATP+H2O; Kd = 10^-12 (tight)

39
Q

bdg change mech for F1 catalysis

A

affin for ATP formed at one cat site red by 10^6 when subst (ADP+Pi) bd to another cat site; pos coop

40
Q

ATP hyrdolysis

A

powers H+ pumping from matrix to IM; allows release of ADP and Pi

41
Q

ATP synthesis

A

H+ moving from IM to matrix through, causes C to rotate; form ATP when tight, release when more ADP and Pi binds and becomes tight

42
Q

oligomycin

A

inhibits H+ mvmt; blocks H+ translocation; [H+] out v in increase to where /\G is positive; oxid stops since H+ mvmt through comps I, III, IV is coupled to e- transfer

43
Q

NBD-Cl

A

inhibits F1 catalysis; eliminates /\p and ATP synth stops b/c E no longer available

44
Q

[ADP]

A

ctrls rate of oxid phos

45
Q

respiratory control ratio (RCR)

A

P:O; indicates coupling efficiency in mito; =active/resting respiration

46
Q

P:O NADH

A

pmf / pmf req to phosphorylate ADP to ATP = 10/4 = 2.5

47
Q

P:O FADH2

A

pmf / pmf req to phosphorylate ADP to ADP = 6/4 = 1.5

48
Q

glucose metabolism

A

686kcal/mol / 7.3kcal/mol to make ATP = 94 mol ATP; efficiency of converting food to ATP is 34%; 94 x 0.34 = 32 mol ATP

49
Q

UCP

A

disengage H+ grad from ATP synth; provide alt path through IM; dissipates pmf as heat (entropic); abundant in brown fat; decrease efficiency of OXPHOS; increase respiration, unctrl’d dissip of H+ grad

50
Q

2,4-DNP

A

enters IMS, becomes protonated, diffuses through lipid bilayer of IM into matrix; can collapse /\p–>unctrl’d fuel oxid; no ATP made; futile cycle of H+ out/in generates heat; used as weight-loss, but lethal (hyperthermia)

51
Q

rotenone

A

complex I; inhibit e-transport, no /\p, no ATP synth

52
Q

amytal

A

complex I; inhibit e-transport, no /\p, no ATP synth

53
Q

piericidin

A

CoQ analog; inhibit e-transport, no /\p, no ATP synth

54
Q

malonate

A

complex II; inhibit e-transport, no /\p, no ATP synth

55
Q

antimycin A

A

complex III; inhibit e-transport, no /\p, no ATP synth

56
Q

cyanide

A

complex IV; inhibit e-transport, no /\p, no ATP synth

57
Q

carbon monoxide

A

complex IV; inhibit e-transport, no /\p, no ATP synth

58
Q

azide

A

complex IV; inhibit e-transport, no /\p, no ATP synth

59
Q

oligomycin

A

inhibits Fo subunit of ATP synthase; blocks respiration; inhibits dissipation of H+ grad, E barrier blocks ET-coupled H+ pumpking; e-stop moving, O2 not reduced to H2O

60
Q

cyanide poisoning

A

can overcome inhib of I, II, or III but NOT IV; antidote kit can restore oxphos (amyl nitrite, Na nitrite, Na thiosulfate)

61
Q

redox shuttles in mito IM

A

carry red equivs from cyto NADH to mito for oxphos

62
Q

glycerol phosphate shuttle

A

most common; NADHcyt oxid provides FADH2 in mito; cyto and mito forms of G3PDH (cyt uses NADH to red DHAP; mito uses FAD to xodi G3P); ignores comp I; regen NAD+

63
Q

malate-aspartate shuttle

A

cyto and mito forms of malate DH and Asp aminotransferase (cyto uses NADH to reduce OAA; mito uses NAD+ to oxid malate); stays where created b/c no OAA/a-KG carrier

64
Q

mtDNA

A

17kb; 13 prots, all rRNA and tRNA to translate them; struc su’s of hyphob, integ memb domains of I, II, IV, V; w/o are rho-0 petites

65
Q

p^0 cells

A

can’t respire, can’t make ATP by oxid phos; still have mito, but different from normal cells

66
Q

mito encephalomyopathies (genetic disease of OXPHOS)

A

caused by mutation in mtDNA; mutation/deletion in prot-coding gene; random deletions (likely tRNA gene, pheno sim to rho^0); severity dep on mutant load (# mutant v normal copies); could have same genetic defect w/diff morphology (go to diff places in diff ppl)

Biochem Unit 2 (13 decks)

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