How Cytochromes with Different Folds Control Heme Redox Potentials†

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

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

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

How cytochromes with different folds control heme redox potentials.

The electrochemical midpoint potentials (E(m)'s) of 13 cytochromes, in globin (c, c(2), c(551), c(553)), four-helix bundle (c', b(562)), alpha beta roll (b(5)), and beta sandwich (f) motifs, with E(m)'s spanning 450 mV were calculated with multiconformation continuum electrostatics (MCCE). MCCE calculates changes in oxidation free energy when a heme-axial ligand complex is moved from water into...

متن کامل

Articles How Cytochromes with Different Folds Control Heme Redox Potentials†

The electrochemical midpoint potentials (Em’s) of 13 cytochromes, in globin (c, c2, c551, c553), four-helix bundle (c′, b562), Râ roll (b5), and â sandwich (f) motifs, with Em’s spanning 450 mV were calculated with multiconformation continuum electrostatics (MCCE). MCCE calculates changes in oxidation free energy when a heme-axial ligand complex is moved from water into protein. Calculated and ...

متن کامل

Electron flow in multiheme bacterial cytochromes is a balancing act between heme electronic interaction and redox potentials.

The naturally widespread process of electron transfer from metal reducing bacteria to extracellular solid metal oxides entails unique biomolecular machinery optimized for long-range electron transport. To perform this function efficiently, microorganisms have adapted multiheme c-type cytochromes to arrange heme cofactors into wires that cooperatively span the cellular envelope, transmitting ele...

متن کامل

Importance of a conserved hydrogen-bonding network in cytochromes c to their redox potentials and stabilities.

To understand the determinants of redox potential and protein stability in c-type cytochromes, we have characterized two mutations to a highly conserved tyrosine group, tyrosine-75, of Rhodobacter capsulatus cytochrome c2. Mutant Y75F was designed to test the importance of the tyrosine hydroxyl group to the typically high redox potentials of the cytochromes c2 while maintaining a hydrophobic co...

متن کامل

Fayet-Iliopoulos Potentials fromFour-Folds

We show how certain non-perturbative superpotentials W̃ (Σ), which are the two-dimensional analogs of the Seiberg-Witten prepotential in 4d, can be computed via geometric engineering from 4-folds. We analyze an explicit example for which the relevant compact geometry of the 4-fold is given by IP fibered over IP. In the field theory limit, this gives an effective U(1) gauge theory with N = (2, 2)...

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

ژورنال

عنوان ژورنال: Biochemistry

سال: 2003

ISSN: 0006-2960,1520-4995

DOI: 10.1021/bi027288k