Subject Index 



657 



Cytochrome c — com. 

 oxidation of 16, 269 



by APS 405-406 

 oxidation-reduction potential 18, 371- 



372, 543 

 polypeptide from 366-367 

 possible linkage in vivo "ill 

 properties of 388-389 

 protein configuration 382-383 

 reactivity with cytochrome h., 511-514 

 reactivity of in oxidative phosphorylation 



389 

 redox potentials of 46, 390-391 



influence of dithionite 391 

 reduction of 379, 545, 554, 576 

 reduction of liaemoprotein in purple 



bacteria 428-429 

 reduction of sulphite and 412-413 

 side chains of 56 



spectra of 42, 57, 105, 152, 171, 410,440 

 structure of 363, 365-368, 384-388 

 structure of bacterial 389-390 

 trapped steady states 454, 457-458 

 Cytochrome c^ 306 



biosynthesis of 216-217 

 effect of cooling on spectrum 446 

 function of in steady state 606-608 

 in plants 483, 498 

 Cytochrome c^, dismutation of formate in 

 411 

 eff"ect on sulphate reduction 404-405 

 evolutionary aspects 416-418 

 function of 415-418 

 haem groups in 415 



function of 415-416 

 in reduction of colloidal sulphur 41 1 

 in sulphate-reducing bacteria 407-414, 



418 

 metabolic function of 411-414 

 molecular weight 409 

 properties of 408-41 1 

 reduction of hydroxylaminc 416 

 spectra of 172,410,415 

 structure of 415 

 sulphate reduction by 413-414 

 thiosulphate reduction and 41 1 

 Cytochrome c^, effect of temperature on 



spectrum 445, 455 

 Cytochrome c^, effect of cooling on 



spectrum 446 

 Cytochrome c'^**, functions 432 

 Cytochrome c derivatives, spectra of 164, 



165 

 Cytochrome c — lactate activity 519 

 Cytochrome c oxidase, activity of 337 

 activity of, effect of concentration of 

 cytochrome c Id^i-ldl 



Cytochrome c, activity of — cont. 



effect of copper and haem content 



286, 287 

 effect of proteins on 267-269 

 effect of cytochrome a + a-^ content 



268 

 effect of salmine on 267, 268, 273, 



279 

 location of substances inhibiting 269- 



assay of 260-275 



composition of 281-299 



copper component of 285-287, 301 



copper content, relationship to haem 



content 286, 287 

 haem component of 283-285 

 haem content, relationship to copper 



content 286, 287 

 inhibition by cytochrome c 275-276 

 lipid content of 287-290 

 oxidation of reduced 297 

 protein content 290 

 reactions of 290-298 



with carbon monoxide 292-294 



with cyanide 295-298 



with ferrocytochrome c 290-291 



with nitric oxide 292-294 



with oxygen 291-292 

 reactivation of 289 

 spectrum of, effect of cyanide 295, 296 

 Cytochrome d 430, 432, 433 

 reactions of molecular oxygen 5 1 

 redox potential 46 

 spectra of 42 

 Cytochromes f, in plants 491, 492 

 Cytochrome o 433-435 

 Cytodeuteroporphyrin 284, 349 



Desulphovibiio desulphuiicans, sulphur 



reduction in 401-408 

 Desulphoviridin, properties of 408^09 



spectrum of 410 

 Detergent solutions, porphyrins solubilized 



in 29^0 

 Deuteroporphyrin, spectra, of 37 

 Diacetyldeutero porphyrins 37 

 Diacetylpyrroporphyrin, spectra of 37 

 Didymium nitrate, spectrum of 439 

 2 : 4-Diformyldeuterohaems, complexes 



formed with bases 74-76 

 Diformyldeutero porphyrin, spectra 37 

 Dimethylamine, complexes formed with 



haem 74, 75, 76 

 Dimethyl mesoporphyrin ester {see Meso- 



porphyrin) 

 Dimethyl protoporphyrin ester {see Proto- 

 porphyrin IX) 



