INDEX 483
biotinylation and, 220–221, 220f
cadmium binding, metallothionein,
174
cystine dimer, 23–24
cytochromes and, 362–363, 373, 384,
384f, 399, 408–411, 427–429, 455
disulfi de bond, 37–38, 37f
fl uorescence resonance energy
transfer (FRET) and, 224–225
iron binding in iron sulfur clusters,
137f, 138, 168–169, 454–456, 457f
modes of interaction with metal ions,
33f
zinc binding in zinc fi ngers, 63–65,
68, 68f, 70f, 72, 72t
C-terminal, 34–35, 35f, 37f, 38, 40, 65,
151, 201–202, 208f, 214, 216, 410,
423,
459
calmodulin and, 303, 303f, 306–326,
309t, 312f, 314 –315t
potassium ion channels and, 208f,
213–214, 216, 218, 220 –233
Curie temperature, 124, 136
Cyclic adenosine monophosphate,
(cAMP), 194, 325
Cytochrome b(6)f
electron transfer, 385–386, 385f
proton translocation, 385f, 386
Q-cycle mechanism, 386, 389–390
Rieske iron sulfur protein (ISP), 22,
383–384, 385f, 386–387, 387t
X-ray crystallography, 383, 385f,
386
Cytochrome bc 1
electron transfer, 388–391, 396–399,
402, 405
inhibitors, 396–404
proton translocation, 389–391,
395–397
Q-cycle mechanism, 396–397
Rieske iron sulfur protein (ISP), 22,
389–391, 394–397, 399, 405
stigmatellin and, 167–170, 385f, 391,
397, 398f, 400t, 402–405, 406f
X-ray crystallography, 399, 405
Cytochrome c
Compound I, 424
Compound II, 424
electron transfer, 405, 408, 410–413,
415 – 416, 420 – 427
ferryl-oxo iron species, see also
compound I, 424
mechanism of activity, 408, 417
proton translocation, 410
X-ray crystallography, 424
Cytochrome c oxidase
bimetallic copper site (CuA), 129–131,
431–432, 433f–434f, 436f, 438
electron transfer and, 5t, 26, 129, 132,
143–146, 426–427, 429–430, 434,
437–439, 449–450, 461
EPR studies, 129–131, 433, 443, 445,
444f
EXAFS studies, 82–83, 442, 444–445
ferryl-oxo iron species, 435, 439
introduction to, 429
mechanism of activity, 439, 443, 453
model compounds, 439–440, 443, 445,
447
proton translocation and, 430, 434
X-ray crystallography, 451–453, 461
Cytochrome c peroxidase, 166, 359,
365–366, 369, 371–372, 377, 410,
421, 424–426, 426f
Cytochrome P450
compound I, 82, 172, 363, 365–368,
365f, 366f, 368f, 371–372, 376–
378, 381
compound II, 366
concerted mechanism, 367–369
electron transfer, 365, 378–379, 378f,
383
ferryl-oxo iron species, see also
compound I, 82, 172, 363–371
model compounds, 372–382
multistep mechanism, 378, 378f
“oxygen rebound” mechanism, 375–
376, 375f
π-cation radical, 364–366, 370, 372,
375–376, 379, 382
X-ray crystallography, 363, 369–372,
370f, 382
Cytoplasm, 55, 96, 200, 408, 428
Ca2+-ATPase and, 327–337
defi nition, 327–328
potassium ion channels and, 204, 213,
216, 221, 224–226, 229–233