✦ LIBER ✦

TDPAC studies of the iron–molybdenum cofactor in nitrogenase

✍ Scribed by C. Pohlmann; H. Appel; W.-G. Thies; A. Müller; K. Schneider; W. Suer

Book ID: 110355420
Publisher: Springer
Year: 1999
Tongue: English
Weight: 81 KB
Volume: 120/121
Category: Article
ISSN: 0304-3843
DOI: 10.1023/a:1017056514222

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Biosynthesis of the nitrogenase iron-mol

Biosynthesis of the nitrogenase iron-molybdenum cofactor

✍ Dennis R. Dean 📂 Article 📅 1995 🏛 Elsevier Science 🌐 English ⚖ 86 KB

Biosynthesis of the iron—molybdenum cofa

Biosynthesis of the iron—molybdenum cofactor of nitrogenase

✍ A.-F. Miller; W.H. Orme-Johnson 📂 Article 📅 1989 🏛 Elsevier Science 🌐 English ⚖ 88 KB

Formation and Insertion of the Nitrogena

Formation and Insertion of the Nitrogenase Iron-Molybdenum Cofactor

✍ Patricia C. Dos Santos; Dennis R. Dean; Yilin Hu; Markus W. Ribbe 📂 Article 📅 2004 🏛 John Wiley and Sons ⚖ 50 KB 👁 1 views

## Abstract For Abstract see ChemInform Abstract in Full Text.

Acetylene reduction by the iron-molybden

Acetylene reduction by the iron-molybdenum cofactor from nitrogenase

✍ Vinod K. Shah; John R. Chisnell; Winston J. Brill 📂 Article 📅 1978 🏛 Elsevier Science 🌐 English ⚖ 242 KB

Exploring the reactivity of the isolated

Exploring the reactivity of the isolated iron-molybdenum cofactor of nitrogenase

✍ B.E. Smith; M.C. Durrant; S.A. Fairhurst; C.A. Gormal; K.L.C. Grönberg; R.A. Hen 📂 Article 📅 1999 🏛 Elsevier Science 🌐 English ⚖ 327 KB

There is strong evidence that the iron-molybdenum cofactor (FeMoco) of nitrogenase forms part of the enzyme's active site. FeMoco, a MoFe 7 S 9 •homocitrate cluster, can be extracted intact from the enzyme into N-methylformamide solution but is reported to be inactive in substrate reduction unless p

A proposal for the function of the iron-

A proposal for the function of the iron-molybdenum cofactor in nitrogenase.

✍ G.N. Schrauzer 📂 Article 📅 1993 🏛 Elsevier Science 🌐 English ⚖ 80 KB