Titlebook: Iron and Copper Proteins; Kerry T. Yasunodu,Howard F. Mower,Osamu Hayaishi Book 1976 The Editor(s) (if applicable) and The Author(s), unde

abracadabra

凶残

GRUEL

PLE

Structural Investigations of the Environment of the Iron-Sulfur Cluster of the 2-Iron Ferredoxinsn-heme”) iron atoms through which electrons are carried. These proteins include the rubredoxins (1), which contain ~50 residues and a single iron, coordinated by 4 cysteines, as shown in Fig. 1A; the “clostridial” ferredoxins (2), possess ~60 residues and 2 active sites of the type shown in Fig. 1B;

ARY

蜿蜒而流

Ophthalmologist

Structural Studies of Electron Transfer Proteins from Sulfate Reducing Bacteria: The Amino Acid Sequshown that a biological reduction of sulfates did occur on this planet as far back as 1 to 2.5 billion years, that is to say before the appearance of the atmospheric oxygen. Sulfate reducing bacteria were for a long time thought to contain a rather truncated electron transfer chain, but recent work

BLUSH

Terminal

Carcinogen

Some Properties of Bovine Pineal Tryptophan Hydroxylaseatalyzed by tryptophan hydroxylase. Since the first demonstration by Grahame-Smith that a specific tryptophan hydroxylase exists in the brain (1), the enzyme has been studied at various laboratories including our own (2–11) and is now accepted as a pterin-dependent aromatic amino acid monooxygenase