656 



Subject Index 



Cytochrome b^, enzymic activity in — cont. 



inhibition of 506 

 extraction of 501-502, 553, 561 

 flavin-protein bonds in 505-507, 569 

 function of 564-565 

 haem-protein link 507-511 

 in yeast, chemical properties of 502-5 1 1 



enzymic activity of 506, 516-519 



enzymic properties of 511-514 



extraction of 501-502 



flavin-protein bonds 505-507, 569 



haem-protein link 507-5 1 1 



kinetics of lactate oxidation 514-520, 

 521-522, 535, 537 



nucleotidc-protein link 511 

 in yeast, properties of 501-522 



prosthetic groups 502-505 



spectrum of 504 

 intramolecular transfer in 566 

 kinetics of lactate oxidation 514-520, 



521-522, 535, 537 

 lactate dehydrogenase activity of 513- 



514, 535, 537 

 nomenclature of 562-563 

 nucleotide-free cytochrome 570-571 

 nucleotide-protein link 5 1 1 

 oxidation-reduction changes 542, 568- 



569 

 problem of 558-560 

 prosthetic groups 502-511 

 protein content 505 

 reduction of 554 



kinetics 565-566 

 relationships 561 



with flavocytochrome bo 559 



with lactate dehydrogenase 501, 553- 

 554, 561 

 reaction of lactate with 568-569 

 reactivity with cytochrome c 511-514 

 reactivity with ferricyanide 511-514 

 reactivity with oxygen 512-514 

 role in respiratory chain 564-565 

 substrate specificity of 511-512, 563-564 

 treatment with /)-chlormercuriphenyl- 



sulphonate 571-572 

 Cytochrome b^ derivatives, absorption 



spectra of 509 

 Cytochrome b-^, in plants 483, 498 

 Cytochrome b^, effect of cooling on 



spectrum 447^48 

 Cytochrome />5, effect of cooling on 



spectrum 448,449,450-451 

 in Uver cells 473, 474 

 Cytochrome b^, in plants 482, 491 

 Cytochrome 67, in plant tissues 482 

 Cytochrome c, activity of effect of cations 



276-280 



Cytochrome c — cont. 

 activity as oxidase 84-87 

 atlinity for hacm 91,92,93 

 amino acids in 90, 363, 365-368, 383- 



384, 410. 415 

 and lactate dehydrogenase 541 

 chemical properties of 55 

 combination with copper 372-380 

 comparative properties of from yeast and 



heart muscle 385-388 

 cooled with liquid nitrogen, effect of 



glycerol on spectrum 442 

 cooled with liquid nitrogen, spectra 440, 



444 

 copper content of 285 

 crystallization of 376-377,414 

 denaturation of 18 

 differences in prosthetic groups 458-459 

 i^'o change 380-381 

 £"0 of in presence of copper 376 

 effect of concentration on activity of 



cytochrome c oxidase 263-267 

 effect of denaturation on E'q values 



390 

 effect on oxidation of lactate 548-549 

 electrometric studies 370-381 

 electron pairing in 20 

 electron transport in 17 

 extraction of 340 



from Rhodospirilhini rubriim 363-368 

 from yeast, oxidation reduction potential 



371-372 

 haemochrome-forming groups in 382-383 

 haemopeptide from 363-368 

 in electron transfer 3 1 3, 552, 604, 605 

 in oxidative phosphorylation 339-342 

 in plant tissue 481,482,498-500 

 in sulphur bacteria 416-418 

 influence on oxidase activity of cyto- 

 chrome a 304 

 influence on oxidation of ascorbic acid 



372-373 

 inhibiting cytochrome c oxidase 275 

 iso-clectric point 385-388 

 leucine aminopeptidase digestion of 383 

 hgand to iron in 390 

 linkage to prosthetic group 382 

 magnetic moment 111 

 metabolism of 216-217 

 modification of 85, 86, 377-380 



effect of temperature on spectrum 

 443^44 



oxidation-reduction titration 378 



protein moieties 84-87 

 native, properties of 388-389 



reactivity of 389 

 optical density ratios 375 



