TheInfoListRev V5.1.84
Xfr/
SummaryRelatedTreeNews

Related topics

Metmyoglobin

Sponsored
Shop Amazon for portable power stations
Browse products on Amazon.
Search Amazon →
As an Amazon Associate I earn from qualifying purchases.

Metmyoglobin is the oxidized form of the oxygen-carrying hemeproteinmyoglobin. Metmyoglobin is the cause of the characteristic brown colouration of meat that occurs as it ages. In living muscle, the concentration of metmyoglobin is vanishingly small, due to the presence of the enzyme , which, in the presence of the cofactorNADH and the coenzymecytochrome b4 converts the Fe in the heme prosthetic group of metmyoglobin back to the Fe of normal myoglobin.

MyoglobinMyoglobinMore reference expression dataBioGPSEnsemblUniProtRefSeq (mRNA)RefSeq (protein)Location (UCSC)Chr 22: 35.61 – 35.64 MbChr 15: 76.9 – 76.93 MbPubMed searchWikidataMyoglobin (symbol Mb or MB) is an iron- and oxygen-binding protein found in the cardiac and skeletalmuscle tissue of vertebrates in general and in almost all mammals. Myoglobin is distantly related to hemoglobin.MuscleMuscleMuscle is a specialised soft tissue, one of the four basic types of animal tissues. There are three types of muscle tissues in vertebrates: skeletal muscle tissue, cardiac muscle tissue, and smooth muscle tissue. Muscle tissue gives skeletal muscles the ability to contract and relax. Muscle tissue contains special contractile proteins called actin and myosin which interact to cause movement.CytochromeCytochromeCytochromes are redox-active proteins containing a heme, with a central iron (Fe) atom at its core, as a cofactor. They are involved in the electron transport chain and redox catalysis. They are classified according to the type of heme and its mode of binding.EnzymeEnzymeLarge biological molecule that acts as a catalystThe enzyme glucosidase converts the sugar maltose into two glucose sugars. Active site residues in red, maltose substrate in black, and NADcofactor in yellow. (PDB: 1OBB​)An enzyme is a biological macromolecule, usually a protein, that acts as a biological catalyst, accelerating chemical reactions without being consumed in the process.Cofactor (biochemistry)Cofactor (biochemistry)A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst. Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound.HemoproteinHemoproteinA hemeprotein (or haemprotein; also hemoprotein or haemoprotein), or heme protein, is a protein that contains a hemeprosthetic group. They are a very large class of metalloproteins. The heme group confers functionality, which can include oxygen carrying, oxygen reduction, electron transfer, and other processes. Heme is bound to the protein either covalently or noncovalently or both.MeatMeatMeat is animal tissue, mostly muscle, that is eaten as food. Humans have hunted and farmed other animals for meat since prehistory. The Neolithic Revolution allowed the domestication of vertebrates, including chickens, sheep, goats, pigs, horses, and cattle, starting around 11,000 years ago. Since then, selective breeding has enabled farmers to produce meat with the qualities desired by producers and consumers.OxygenOxygenChemical element with atomic number 8 (O)–↑O↓Snitrogen ← oxygen → fluorineIronIronChemical element with atomic number 26 (Fe)–↑Fe↓Rumanganese ← iron → cobaltRedoxRedoxRedox ( RED-oks, REE-doks, reduction–oxidation or oxidation–reduction) is a type of chemical reaction in which the oxidation states of the reactants change. Oxidation is the loss of electrons or an increase in the oxidation state. Reduction is the gain of electrons or a decrease in the oxidation state. The oxidation and reduction processes occur simultaneously in the chemical reaction. Redox reactions fall into two classes.Nicotinamide adenine dinucleotideNicotinamide adenine dinucleotideCoenzymeChemical compoundNicotinamide adenine dinucleotide (NAD+) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adeninenucleobase and the other, nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD and NADH (H for hydrogen), respectively.

*As an Amazon Associate I earn from qualifying purchases.

AboutPrivacyContact

TheInfoList organizes topic information and links to original sources.

Loading topic…