Ligand discrimination of myoglobin in solution: an iron L-edge X-ray absorption study of the active centre.

نویسندگان

  • Kathrin M Lange
  • Ronny Golnak
  • Sébastien Bonhommeau
  • Emad F Aziz
چکیده

Iron L-edge X-ray absorption spectra of the active centre of myoglobin in the met-form, in the reduced form and upon ligation to O2, CO, NO and CN are presented. The strength of ligation with the iron centre is finger-printed through the variation of the L3 : L2 intensity ratio. Charge Transfer Multiplet calculations are performed and give qualitative information about oxidation states as well as charge transfer.

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

Iron L-Edge X-ray Absorption Spectroscopy of Myoglobin Complexes and Photolysis Products

We demonstrate the first application of L-edge X-ray absorption spectroscopy (XAS) to the electronic characterization of biological photolysis products. The experimental L-edge XAS spectra of deoxymyoglobin (deoxy Mb), oxymyoglobin (MbO2), carbonmonoxymyoglobin (MbCO), and the low-temperature photoproducts (Mb*CO and Mb*O2) are presented and compared to simulated spectra using a ligand field mu...

متن کامل

X-ray structure analysis of a metalloprotein with enhanced active-site resolution using in situ x-ray absorption near edge structure spectroscopy.

X-ray absorption spectroscopy is exquisitely sensitive to the coordination geometry of an absorbing atom and therefore allows bond distances and angles of the surrounding atomic cluster to be measured with atomic resolution. By contrast, the accuracy and resolution of metalloprotein active sites obtainable from x-ray crystallography are often insufficient to analyze the electronic properties of...

متن کامل

Soft X-ray emission spectroscopy at the L-edge of transition metals in metalloproteins

Soft X-ray emission spectroscopy of aqueous myoglobin upon Fe 2p core excitation was carried out using a liquid cell with a 150 nm-thick polyimide window in a high vacuum chamber below 1×10−7 Pa. Fe 2p soft X-ray emission from the heme center of a met-myoglobin powder was effectively detected compared to that of an Fe2O3 powder. Fe 2p soft X-ray emission spectra for a series of aqueous-myoglobi...

متن کامل

Fluoride Precipitation of Cu Over Fe in a Selected pH Window

Fe is an impurity in most leach liquors. Its coexistence with copper in leaching solution of chalcopyrite (CuFeS2) which is the most important mineral of copper creates major extraction problems. Hydrochloric acid dissolves both copper and iron during chloride leaching of this mineral. Separation of Fe from Cu is thus necessary to obtain pure copper. This paper presents a novel metho...

متن کامل

Probing the electronic and geometric structure of ferric and ferrous myoglobins in physiological solutions by Fe K-edge absorption spectroscopy.

We present an iron K-edge X-ray absorption study of carboxymyoglobin (MbCO), nitrosylmyoglobin (MbNO), oxymyoglobin (MbO2), cyanomyoglobin (MbCN), aquomet myoglobin (metMb) and unligated myoglobin (deoxyMb) in physiological media. The analysis of the XANES region is performed using the full-multiple scattering formalism, implemented within the MXAN package. This reveals trends within the heme s...

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:
  • Chemical communications

دوره 49 39  شماره 

صفحات  -

تاریخ انتشار 2013