Synthetic analogs of the active sites of iron-sulfur proteins. 8. Some electronic properties of (Fe4S4(SR)4)3-, analogs of reduced bacterial ferredoxins.

نویسندگان

  • R B Frankel
  • T Herskovitz
  • B A Averill
  • R H Holm
  • P J Krusic
  • W D Phillips
چکیده

One-electron reduction of the synthetic tetramers [FemSa(SR)~] 2(R CHgPh, Ph), by chemical and electrochemical methods affords the corres~ofiding-trianions. ~The collective results from optical, electron paramagnetic resonance, and M~ssbauer spectroscopy, when compared to available data for reduced 4-Fe and 8-Fe ferredoxi~ proteins and super-reduced Chromatium high-potential protein, reveal that [FeASa(SR)j are electronic analogs of the [Fe4S4(S-Cys) 4] active sites of these prot~ifis. "

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

SBAUER PROPERTIE s OF SYNTHETIC ANALOGS OF ACTIVE SITES OF THE IRON-SULFUR PROTEINS

Mossbauer spectroscopy of the synthetic tetramers [Fe4S4(SR)4]2(R = alkyl, aryl) and the corresponding trianions obtained by one-electron reduction, when compared with available data for 4-Fe and 8-Fe iron-sulfur proteins, shows that these tetramers are electronic analogs of the active sites of the proteins.

متن کامل

Synthetic analogs of the active sites of iron-sulfur proteins. Structure and properties of bis(o-xylyldithiolato-m2-sulfidoferrate (3)), an analog of the 2Fe-2S proteins.

The synthetic analog approach has been applied to a clarification of the active sites of 2Fe-2S(*) proteins. The compound (Et(4)N)(2)[FeS(SCH(2))(2)C(6)H(4)](2), derived from o-xylyl-alpha,alpha'-dithiol, has been prepared and its structure has been determined by x-ray diffraction. The centrosymmetric anion contains two tetrahedrally coordinated ferric ions bridged by two sulfide ions and separ...

متن کامل

Iron-sulfur proteins, present in animals, plants, and bacteria, are metalloproteins which play important roles as electron car

Iron-sulfur clusters, functioning primarily as electron transfer agents, have important roles in biology, participating in plant photosynthesis, nitrogen fixation, steroid metabolism, and oxidative phosphorylation. Present in animals, plants, and bacteria, iron-sulfur clusters are found at the active sites of redox and catalytic proteins. Since the 1970s, metal sites in iron-sulfur proteins hav...

متن کامل

Iron–Sulfur Models of Protein Active Sites

Iron–sulfur clusters appear in a great many proteins as both electron-transport and enzymatic sites (see Iron–Sulfur Proteins); for this reason there has been great interest for 30 years in the development and understanding of iron–sulfur model complexes. Both structure and properties of synthetic analogs of 1-, 2-, 3-, and 4-iron protein active sites have been studied extensively.1 This articl...

متن کامل

Structure and properties of a synthetic analogue of bacterial iron--sulfur proteins.

The compound (Et(4)N)(2)[Fe(4)S(4)(SCH(2)Ph)(4)] has been prepared and its structure determined by x-ray diffraction. The Fe(4)S(4) core of the anion possesses a configuration of D(2d) symmetry that is closely related to the Fe(4)S(4) active-site structures of the high-potential iron protein from Chromatium and the ferredoxin from Micrococcus aerogenes. Electronic properties of the tetrameric a...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Biochemical and biophysical research communications

دوره 58 4  شماره 

صفحات  -

تاریخ انتشار 1974