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The subunit of hemoglobin is a protein molecule made up of four polypeptide chains. These chains consist of two alpha chains and two beta chains, each with a heme group that contains iron, which binds to oxygen.
The organometallic iron compound found in hemoglobin is called heme. Heme is a complex of iron and a porphyrin molecule, specifically protoporphyrin IX, which is responsible for binding oxygen in red blood cells.
Hemoglobin is a protein found in red blood cells that functions to transport oxygen throughout the body. It is composed of a heme group, which contains iron and binds with oxygen, and globin chains, which provide the structure for the heme groups. The interaction between heme and globin allows hemoglobin to efficiently transport oxygen from the lungs to the body's tissues.
The breakdown product of heme is bilirubin. Bilirubin is produced when heme is broken down in the liver as a part of the normal process of recycling heme from old red blood cells.
The heme group within the hemoglobin molecule is what actually binds to the oxygen molecule. This process involves the iron atom within the heme group forming a reversible coordination bond with the oxygen molecule.
The coordination number is six. Four of these sites are occupied by the nitrogens in the heme moiety, one is occupied by the nitrogen in the side chain of a histidine residue, and the remaining one is occupied by a loosely bound oxygen molecule.
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iron
iron
Nitrate reductase does not contain the prosthetic group heme. Instead, it typically contains molybdenum cofactor (Moco) and heme iron-sulfur center as prosthetic groups.
Heme is a ferrous ion prosthetic group (Fe2+) present in metalloproteins or specifically Hemoproteins such as Hemoglobin, porphyrin. heme is also found in proteins such as myoglobin, catalase, cytochromes. In these proteins Heme either participates in the catalysis or act as a stabilizer of active site amino acid.
Hemoglobin contains a heme group with an Iron ion attached to it. This iron is what binds to O2.
A portion of the heme group
Oxygen attaches to heme through coordination bonding. The iron atom at the center of heme forms a reversible bond with oxygen, creating oxyhemoglobin. This interaction is crucial for oxygen transport in the blood.
The subunit of hemoglobin is a protein molecule made up of four polypeptide chains. These chains consist of two alpha chains and two beta chains, each with a heme group that contains iron, which binds to oxygen.
The organometallic iron compound found in hemoglobin is called heme. Heme is a complex of iron and a porphyrin molecule, specifically protoporphyrin IX, which is responsible for binding oxygen in red blood cells.