Section 1, paragraph 2, last sentence: for has become opportune, read is timely.
Section 1, paragraph 4 (excluding notes), sentence 1: for as far as unambiguously known, read as far as is unambiguously known.
Section 4.2, paragraph 2. Reference 11 as well as reference 10 applies here.
Section 4.2, Table 1, change heading of column three to Solubility of product from treatment of cytochrome with acetone-HCl in ether
Section 4.2, paragraph 1 of c), added last sentence: Note. The value of 550.25 nm stems from early work and may need revision; a value redetermined carefully is 499.9 nm (G. Palmer, personal communication).
Section 4.2, penultimate paragraph, sentence 6: for (EPR, formerly also called electron spin resonance, ESR). read (EPR, also called electron spin resonance, ESR).
Section 4.2, penultimate paragraph, sentence 6: for complex cytochrome a and heme protein systems, read complex heme-protein systems.
Section 5.1, paragraph 2, sentence 1: for gained wide acceptance, read gained acceptance.
Section 5.2 title: for Simple Iron-Sulfur Protein, read Simple Iron-Sulfur Proteins.
Scheme 1: the third box from the left in the bottom row should read (Iron-sulfur molybdenum) flavoproteins.
Section 5.3.1 (b) the footnote referred to in the last sentence is 9 (not 10).
Section 5.3.2 (a) sentence 2: for a two-iron two-labile-sulfur cluster, read a two-iron, two-labile-sulfur cluster; and for a four-iron four-labile-sulfur cluster, read a four-iron, four-labile-sulfur cluster.
Section 5.3.2 (a) penultimate sentence. add ferredoxin or iron-sulfur protein at the end.
Section 5.3.2 (a) the footnote referred to in the last sentence is 10 (not 11).
Section 7.1, first sentence of text: replace by Molybdenum enzymes contain molybdenum at the catalytic center responsible for reaction with substrate.
Section 10, paragraph a), sentence 1: for methanol dehydrogenases, read methanol dehydrogenase.
Section 10, paragraph a), last sentence: replace by Its cofactor contains a tryptophan dimer (ref 46) with one indole ring oxidized to the o-quinone group.
The version of this document first published in Eur. J. Biochem., 1991, 200, 599-611 was reprinted by an offset process in J. Biol. Chem., 267, 665-677 (1992). It was also reproduced retaining the original EJB page numbers in Biochim. Biophys. Acta, 1991, 1060, between page 236 and 237. Corrections were published in Eur. J. Biochem., 1993, 213, 2-3. Three additional corrections have been marked with an asterisk below. (This list repeats all relevant ones listed above.)
|599||665||1||contents, item 5.2||for iron-sulfur protein, read iron-sulfur proteins.|
|599||665||1||line 8 up||for a number of enzyme, read a number of enzymes.|
|599||665||1||line 2||for has become opportune, read is timely.|
|600||666||1||paragraph 2, line 3||for as far as unambiguously known, read as far as is unambiguously known.|
|600||666||1||paragraph 2, line 8||for ubiquinol/ cytochrome-c reductase, read ubiquinol-cytochrome-c reductase.|
|600||666||2||paragraph 2. line 3||for oxidationreductions, read oxidation-reduction reactions.|
|600||666||2||last line||for The dehydrogenase the, read The dehydrogenase then.|
|601*||667||2||Paragraph 2 of 4.2||for  read [10,11]|
|602*||668||1/2||Table 1, heading of column three||for Solubility of product treatment, read Solubility of product from treatment.|
|602||668||1||line 12 up||for methylethylketone, read methyl ethyl ketone.|
|602||668||1||line 8 up||for the extracted, read then extracted.|
|602||668||1||last line||for to the systemic name, read to the systematic name.|
|602||668||2||first paragraph of c), last-but-one line||for wavelength maximum, read wavelength maximum. Note. The value of 550.25 nm stems from early work and may need revision; a value redetermined carefully is 499.9 nm (G. Palmer, personal communication).|
|603||669||1||lines 8/9||for (EPR, formerly also called electron spin resonance, ESR). read (EPR, also called electron spin resonance, ESR).|
|603||669||1||lines 9/10||for complex cytochrome a and heme protein systems, read complex heme-protein systems.|
|603||669||1||section 4.3, first|
paragraph, last line
|for revised list of cytochrome. read revised list of cytochromes.|
|603||669||2||section 4.4.1. line 3||for two hemes A, read two hemes a.|
|603||669||2||section 4.4.1 line 13||for (see section 6.5, read (see section 6.5).|
|604||670||1||last two lines||for respiractory chain, read respiratory chain.|
|604||670||2||line 14 up||for functions like cytochrome c, read functions like cytochrome c2|
paragraph 2, lines 1/2
|for gained with acceptance, read gained acceptance.|
|605||671||2||footnote 9, line 10||for one electron more or more electron less, read one electron more or one electron less.|
|606||672||1||subtitle 5.2||for SIMPLE IRON-SULFUR PROTEIN, read SIMPLE IRON-SULFUR PROTEINS.|
|606||672||1||subtitle 5.2.2||for Ferredoxin. read Ferredoxins.|
|606||672||1||subtitle 5.2.3||for iron-sulfur protein. read iron-sulfur proteins.|
|606||672||2||paragraph c), lines 8/9||for or bc-1, read or bc-1, and for more complex system, read more complex systems.|
|606||672||2||section 5.3.2, line 5||for a four-iron-labile-sulfur cluster, read a four-iron, four-labile-sulfur cluster.|
|606||672||2||footnote 10, line 12||for When there the Fe/S stoichiometry, read When the Fe/S stoichiometry.|
|607||673||in the Scheme||the third box from the left in the bottom row should read (Iron-sulfur molybdenum) flavoproteins.|
|607*||673||1||line 3||for 'three-iron-four-sulfur'. read 'three-iron-four-sulfur' ferredoxin or iron-sulfur protein.|
|607||673||1||paragraph c), line|
preceding the comment
|for 2[4Fe-4S]2+ :2[Fe-4S]1+, read 2[4Fe-4S]2+ :2[4Fe-4S]1+|
|607||673||2||line 13||for [4Fe-4S]2+(+:1+), read [4Fe-4S]2+(2+:1+).|
|607||673||2||paragraph e), line 13 up||for detectable by the EPR measurements, read detectable by EPR measurements.|
lines 7/8 of text:
|for does not greatly changes, read does not greatly change.|
|608||674||2||line 3||for divided into low classes, read divided into two classes.|
paragraph 3, line 3
|for plasticyanin, read plastocyanin.|
|608||674||2||line 3 up||for their true biological functions, read their true biological function.|
|609||675||1||section 6.2, lines 8/9 of text||for last group may may also, read last group may also.|
|609||675||1||section 6.5, line 5 of text||for has been refererd to, read has been referred to.|
first sentence of text
|replace by Molybdenum enzymes contain molybdenum at the catalytic center responsible for reaction with substrate.|
|610||676||1||section 10, paragraph a), lines 2/3||for methanol dehydrogenases, read methanol dehydrogenase.|
|610||676||1||section 10, paragraph a), lines 11/12||replace by Its cofactor contains a tryptophan dimer  with one indole ring oxidized to the o-quinone group.|
|610||676||1||paragraph b), first sentence||for The only bacterial quinoprotein oxidase, read The only bacterial quinoprotein oxidase known.|