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Items: 13

1.

Metalloproteins

Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)

Year introduced: 1973

2.

Protein Binding

The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.

Year introduced: 1970(1966)

3.

Nonheme Iron Proteins

Proteins, usually acting in oxidation-reduction reactions, containing iron but no porphyrin groups. (Lehninger, Principles of Biochemistry, 1993, pG-10)

Year introduced: 1997

4.

Chemistry, Bioinorganic

Field of chemistry pertaining to the study of inorganic compounds or ions and their interactions with biological ligands at the molecular level.

Year introduced: 1989

5.

Spectroscopy, Mossbauer

A spectroscopic technique which uses the Mossbauer effect (inelastic scattering of gamma radiation resulting from interaction with heavy nuclei) to monitor the small variations in the interaction between an atomic nucleus and its environment. Such variations may be induced by changes in temperature, pressure, chemical state, molecular conformation, molecular interaction, or physical site. It is particularly useful for studies of structure-activity relationship in metalloproteins, mobility of heavy metals, and the state of whole tissue and cell membranes.

Year introduced: 1989

6.

Metallothionein

A low-molecular-weight (approx. 10 kD) protein occurring in the cytoplasm of kidney cortex and liver. It is rich in cysteinyl residues and contains no aromatic amino acids. Metallothionein shows high affinity for bivalent heavy metals.

Year introduced: 1984(1975)

7.

Iron-Sulfur Proteins

A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.

Year introduced: 1991(1977)

8.

Hemocyanins

Metalloproteins that function as oxygen transport proteins in the HEMOLYMPH of MOLLUSKS and ARTHROPODS. They are characterized by two copper atoms, coordinated with HISTIDINE residues, that reversibly bind a single oxygen molecule; they do not contain HEME groups.

Year introduced: 2018 (1964)

9.

Hemerythrin

A non-heme iron protein consisting of eight apparently identical subunits each containing 2 iron atoms. It binds one molecule of oxygen per pair of iron atoms and functions as a respiratory protein.

Year introduced: 1991(1975)

10.

Azurin

A bacterial protein from Pseudomonas, Bordetella, or Alcaligenes which operates as an electron transfer unit associated with the cytochrome chain. The protein has a molecular weight of approximately 16,000, contains a single copper atom, is intensively blue, and has a fluorescence emission band centered at 308nm.

Year introduced: 1991(1975)

11.

Adrenodoxin

An iron-sulfur protein which serves as an electron carrier in enzymatic steroid hydroxylation reactions in adrenal cortex mitochondria. The electron transport system which catalyzes this reaction consists of adrenodoxin reductase, NADP, adrenodoxin, and cytochrome P-450.

Year introduced: 1975

12.

cysteine desulfurase [Supplementary Concept]

pyridoxal phosphate enzyme which catalyzes the formation of L-alanine and elemental sulfur from cysteine; required for full activation of the metalloproteins; do not confuse with CsdA protein, E coli

Date introduced: April 30, 1993

13.

Heme-Binding Proteins

Metalloproteins that contain a HEME ligand as the prosthetic group.

Year introduced: 2020(1984)

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