[HTML][HTML] The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin

D Hamdane, L Kiger, S Dewilde, BN Green… - Journal of Biological …, 2003 - ASBMB
Neuroglobin and cytoglobin reversibly bind oxygen in competition with the distal histidine,
and the observed oxygen affinity therefore depends on the properties of both ligands. In the …

[HTML][HTML] A robust zirconium amino acid metal-organic framework for proton conduction

…, J Marrot, C Martineau-Corcos, D Hamdane… - Nature …, 2018 - nature.com
Proton conductive materials are of significant importance and highly desired for clean
energy-related applications. Discovery of practical metal-organic frameworks (MOFs) with high …

[HTML][HTML] Structure and function of an NADPH-cytochrome P450 oxidoreductase in an open conformation capable of reducing cytochrome P450

D Hamdane, C Xia, SC Im, H Zhang, JJP Kim… - Journal of biological …, 2009 - ASBMB
NADPH-cytochrome P450 oxidoreductase (CYPOR) catalyzes the transfer of electrons to all
known microsomal cytochromes P450. A CYPOR variant, with a 4-amino acid deletion in the …

Oxygen activation by cytochrome P450 monooxygenase

D Hamdane, H Zhang, P Hollenberg - Photosynthesis research, 2008 - Springer
Unlike photosystem II (PSII) that catalyzes formation of the O–O bond, the cytochromes P450
(P450), members of a superfamily of hemoproteins, catalyze the scission of the O–O bond …

[HTML][HTML] Conformational changes of NADPH-cytochrome P450 oxidoreductase are essential for catalysis and cofactor binding

C Xia, D Hamdane, AL Shen, V Choi, CB Kasper… - Journal of Biological …, 2011 - ASBMB
The crystal structure of NADPH-cytochrome P450 reductase (CYPOR) implies that a large
domain movement is essential for electron transfer from NADPH via FAD and FMN to its redox …

The crystal structure of wild-type human brain neuroglobin reveals flexibility of the disulfide bond that regulates oxygen affinity

BG Guimarães, D Hamdane, C Lechauve… - … Section D: Biological …, 2014 - scripts.iucr.org
Neuroglobin plays an important function in the supply of oxygen in nervous tissues. In human
neuroglobin, a cysteine at position 46 in the loop connecting the C and D helices of the …

Dihydrouridine in the transcriptome: new life for this ancient RNA chemical modification

…, Y Motorin, M Helm, D Hamdane - ACS Chemical …, 2022 - ACS Publications
Until recently, post-transcriptional modifications of RNA were largely restricted to noncoding
RNA species. However, this belief seems to have quickly dissipated with the growing …

[HTML][HTML] Neuroglobin and other hexacoordinated hemoglobins show a weak temperature dependence of oxygen binding

…, T Burmester, T Hankeln, L Moens, D Hamdane… - Biophysical journal, 2004 - cell.com
Mouse and human neuroglobins, as well as the hemoglobins from Drosophila melanogaster
and Arabidopsis thaliana, were recombinantly expressed in Escherichia coli, and their …

[HTML][HTML] Cytochrome b5 inhibits electron transfer from NADPH-cytochrome P450 reductase to ferric cytochrome P450 2B4

H Zhang, D Hamdane, SC Im, L Waskell - Journal of biological chemistry, 2008 - ASBMB
Experiments demonstrating that cytochrome (cyt) b 5 inhibits the activity of cytochrome P450
2B4 (cyt P450 2B4) at higher concentrations suggested that cyt b 5 was occupying the cyt …

[HTML][HTML] The UbiK protein is an accessory factor necessary for bacterial ubiquinone (UQ) biosynthesis and forms a complex with the UQ biogenesis factor UbiJ

…, SB Hernández, B Faivre, D Hamdane… - Journal of Biological …, 2017 - ASBMB
Ubiquinone (UQ), also referred to as coenzyme Q, is a widespread lipophilic molecule in
both prokaryotes and eukaryotes in which it primarily acts as an electron carrier. Eleven …