INDEX 495
ribozymes and, 241–242, 247,
247–249, 248t, 253–263, 259t,
264f, 265f, 268, 273, 274f, 281,
285–286, 289–294, 291t, 296–299,
333
sequencing and, 58–59, 149
transcription and, 55(^18) O labeling, proteomic studies, 42–43
Oligonucleotides:
catalytic RNA (ribozymes) and, 240f,
245
mass spectrometry, sequencing and,
14 8 –150
zinc fi nger protein and, 66
Organometallic chemistry, see
Bioorganometallic chemistry
Orbitals:
highest occupied molecular (HOMO)
lowest unoccupied molecular
(LUMO)
Slater-type (STO)
Outer-sphere (OS):
electron transfer, 10, 23–25
reaction rates, 11–12
Oxidation, metals in biological systems,
2–5
Oxidation-reduction, 14, 23
electron transfer and, 22–26
Oxidation state:
copper ions in cytochromes, 443
copper ions in methane
monooxygenase, 463– 465
iron ions in hemoglobin, 349
iron ions in cytochromes, 359, 360,
363, 366–367, 369, 373, 412–414,
426, 428, 445
iron ions in iron-sulfur clusters, 4, 24
metals in biological systems, 2–5, 4t,
5t, 6t, 14, 19
nuclear magnetic resonance and, 103
Mössbauer isomer shift (δ) and, 134,
135t
nitrogenase Mössbauer isomer shift
(δ) and, 138–139
X-ray absorption energy and, 79,
81–82
Oxidoreductaes, 45, 167, 212, 214, 229,
361, 388, 411
Oxygen, O 2 :
insertion enzymes, see also
cytochrome P450, methane
monooxygenase, 22, 82, 172
molecular orbital diagram, 349f
percent composition of human body,
2t
reduction enzymes, see also specifi c
cytochromes, 24, 82, 143
transport proteins, see also
hemoglobin, myoglobin,
hemocyanin, 4, 5t, 30, 43, 83, 90 –
91, 135t, 146 –147, 192–193,
343–349
solubility, 344
Oxygenation: see also methane
monooxygenase, cytochrome
P450
cytochrome P450, 365, 365f, 378
methane monooxygenase, 22,
459–460
Oxy-heme stereochemistry, 351–352,
351t, 352t
Oxyhemoglobins, see hemoglobin, oxy-
Oxymyoglobin, see myoglobin, oxy-
Palladium (Pd), 7t, 16
Paramagnetism, 17, 102–104, 108, 122,
125–129, 136–138, 153, 243, 288–
289, 348, 362–263, 376, 460
Parkinson’s disease, 160
PASCAL, 185
Passive diffusion, 193, 195–197
Peptide bonds, formation of, 33–34, 34f
Peroxidase, 82, 366, 372–373, 377, 380
cytochrome c peroxidase, 166, 359,
363, 365–366, 371–372, 377, 410,
421,
424–426, 426f, 429
Peroxide ion, see anions
Peroxo ligand(s), see also cytochrome c
oxidase, cytochrome c
peroxidase, cytochrome P450, 82,
166, 363, 365f, 366f, 368, 368f,
372, 374, 374f, 382, 433, 439, 441f,
443–445, 451
pH, 190t
cytochromes and, 360, 385, 402, 408,
418, 420, 424, 437–439