Heme protein biosensors
✍ Scribed by Michael K. Chan
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 122 KB
- Volume
- 04
- Category
- Article
- ISSN
- 1088-4246
No coin nor oath required. For personal study only.
✦ Synopsis
The recent discovery that heme proteins can serve as molecular biosensors has opened up a new direction in heme biochemistry directed towards elucidating their structure-function relationships. Examples of such sensory heme proteins include the FixL proteins of Rhizobia involved in oxygen sensing, the CooA protein of Rhodospirillum rubrum that senses CO, and the mammalian soluble guanylate cyclase—the only proven nitric oxide receptor. This overview summarizes the current state of knowledge regarding the roles and mechanisms of these novel proteins and discusses the evidence for other putative heme protein sensors. These topics will be presented in the Heme Protein Biosensors Symposium at the First International Conference of Porphyrins and Phthalocyanines in Dijon, France.
📜 SIMILAR VOLUMES
## Abstract __In silico__ screening has become a valuable tool in drug design, but some drug targets represent real challenges for docking algorithms. This is especially true for metalloproteins, whose interactions with ligands are difficult to parametrize. Our docking algorithm, EADock, is based o
if they have questions to contribute or if they can provide answers to questions that are provided here from time to time. In the latter case, instructions will be sent to interested readers. Answers should be, whenever possible, evidence-based and provide relevant references.
## Abstract It is shown by using the vibronic approach that the iron displacement out of the porphyrin plane in deoxyheme proteins intermixes the porphyrin π and axial iron–histidine σ electronic subsystems. This intermixing explains the substantial coupling of the iron–histidine vibration to the h
## Abstract Heme proteins that have been reconstituted with certain hemins may contain substantial fractions of a minor component in which the orientation of the heme in the folded pocket differs from the major (“native”) conformation by a 180° rotation about the α‐γ meso axis. In fact, this minor
## Abstract Heme scavenging by plasma proteins, including serum albumin (SA), provides protection against free‐heme oxidative damage, limits access by pathogens to the heme, and contributes to iron homeostasis by recycling the heme iron. In turn, serum heme‐albumin (SA‐heme) acquires heme‐based lig