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Biochem Unit 2 > Ackerman Lectures 5-8 > Flashcards

Ackerman Lectures 5-8 Flashcards

(66 cards)

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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
complex II rxn
succinate --> FAD; FADH2-->(FeS)3-->Cyt b --> CoQ; must rel 2 e- at once
26
NADH shuttle (G3PDH)
G3P-->FAD; FADH2-->CoQ; must rel 2 e- at once
27
b-oxid path (FA-CoADH)
FA-CoA -->FAD; FADH2-->CoQ; must rel 2 e- at once
28
NADH as substrate
IMS: matrix is 10 per 2e- transferred (pmf=10)
29
SUC or FA-CoA or Gly3P as substrate
IMS: matrix is 6 per 2e- transferred (pmf =6)
30
respiration proton gradient
chem (pH) and charge gradients w/IMS more positive than matrix; contrib to change in free E as pmf (excess protons in IMS)
31
ATP synthase
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
F1
peripheral memb prot catalytic sites (3); a3b3y3e
33
F0
integral memb prot proton channel; d+ab2c10
34
catalytic head of ATP synthase
a3b3; catalytic site in each of 3 b subunits interfaces
35
proton pump of ATP synthase
a(c ring); H+ transloc causes to rotate
36
ATP synthase rotor
ye; att to c ring; rotate in unison
37
ATP synthase stator
b2d + d; prevents rotation of a3b3 head gp
38
Keq of ATP hydrolysis
1; cat coop b/w 3 sites; freely reversible; ATP+H2O-->ADP+Pi and ADP+Pi-->ATP+H2O; Kd = 10^-12 (tight)
39
bdg change mech for F1 catalysis
affin for ATP formed at one cat site red by 10^6 when subst (ADP+Pi) bd to another cat site; pos coop
40
ATP hyrdolysis
powers H+ pumping from matrix to IM; allows release of ADP and Pi
41
ATP synthesis
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
oligomycin
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
NBD-Cl
inhibits F1 catalysis; eliminates /\p and ATP synth stops b/c E no longer available
44
[ADP]
ctrls rate of oxid phos
45
respiratory control ratio (RCR)
P:O; indicates coupling efficiency in mito; =active/resting respiration
46
P:O NADH
pmf / pmf req to phosphorylate ADP to ATP = 10/4 = 2.5
47
P:O FADH2
pmf / pmf req to phosphorylate ADP to ADP = 6/4 = 1.5
48
glucose metabolism
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
UCP
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
2,4-DNP
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
rotenone
complex I; inhibit e-transport, no /\p, no ATP synth
52
amytal
complex I; inhibit e-transport, no /\p, no ATP synth
53
piericidin
CoQ analog; inhibit e-transport, no /\p, no ATP synth
54
malonate
complex II; inhibit e-transport, no /\p, no ATP synth
55
antimycin A
complex III; inhibit e-transport, no /\p, no ATP synth
56
cyanide
complex IV; inhibit e-transport, no /\p, no ATP synth
57
carbon monoxide
complex IV; inhibit e-transport, no /\p, no ATP synth
58
azide
complex IV; inhibit e-transport, no /\p, no ATP synth
59
oligomycin
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
cyanide poisoning
can overcome inhib of I, II, or III but NOT IV; antidote kit can restore oxphos (amyl nitrite, Na nitrite, Na thiosulfate)
61
redox shuttles in mito IM
carry red equivs from cyto NADH to mito for oxphos
62
glycerol phosphate shuttle
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
malate-aspartate shuttle
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
mtDNA
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
p^0 cells
can't respire, can't make ATP by oxid phos; still have mito, but different from normal cells
66
mito encephalomyopathies (genetic disease of OXPHOS)
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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