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The d electron configuration can be calculated by taking the valence electrons and subtracting the oxidation state for iron in heme this would be eight minus two equaling six.

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There a four isomers of heme all of which can be found within different protein structures, the differences between the isomers are seen in the vinyl side chain of the heme. A heme is not chiral as it can not be layered over a mirror image of it's self.

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Two common ligands that can bind and unbind to the heme are O2 and CO2, these ligands are what makes hemes so important in the structure of hemoglobin as they are what allows red blood cells to carry O2 around the body and to bring CO2 back to the lungs to then be exhaled. While no O2 molecules are bound to a heme the Fe2+ atom at the center of the structure is +2, when oxygen is bound to a hemoglobin it is refereed to as a Oxyhemoglobin and retains it's +2 state. [4]

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The heme contains a Fe2+ at the center with a octahedral geometry while in an oxygenated state, with the coordination number being four due to the number of the surrendering nitrogen.

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The presence of of CO or CN when bound to a heme causes the binding affinity for O2 to change. When CO is bound the binding affinity for O2 increases which prevents the O2 from unbinding from the heme, while the CN lowers the binding affinity which prevents O2 from binding to the heme at all.

Chart of effects of Toxins on hemes, acquired from: https://pubs.rsc.org/en/content/articlelanding/2019/cp/c9cp02583a/unauth#!divAbstract

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1. Hooda, J., Shah, A., & Zhang, L. (2014). Heme, an Essential Nutrient from Dietary Proteins, Critically Impacts Diverse Physiological and Pathological Processes. Nutrients, 6(3), 1080-1102. doi: 10.3390/nu6031080

2.Metal Complex in the Blood. (2021). Retrieved 1 February 2021, from http://www.chemistry.wustl.edu/~edudev/LabTutorials/Hemoglobin/MetalComplexinBlood.html

3.  Poulos, T. (2014). Heme Enzyme Structure and Function. Chemical Reviews, 114(7), 3919-3962. doi: 10.1021/cr400415k

4. Kassa, T., Jana, S., Meng, F., & Alayash, A. (2016). Differential heme release from various hemoglobin redox states and the upregulation of cellular heme oxygenase‐1. FEBS Open Bio, 6(9), 876-884. doi: 10.1002/2211-5463.12103

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The heme is a metalloprotein that is a major component of the hemoglobin which is found within blood, the heme allows for oxygen to be carried through the blood stream making it a integral part of life [3]. A heme consist of a organic compounds called the porphyrin as well as an iron (Fe (II)) atom at center, this iron is what allows for oxygen to bind to the heme. There are four hemes found within a hemoglobin for the transportation of oxygen, when oxygen binds with the heme a conformational change takes place that causes the whole protein to change it's shape [2]. The abundance of heme in the body is astronomical as 4 hemes are present within a single hemoglobin with an approximate of 270 million hemoglobin in a single red blood cells with the amount of hemes totaling at over a billion hemes in every red blood cell in the human body. The iron that can be absorbed through the consumption of food comes in 2 forms refereed to as heme and non-heme, heme iron is often found within meat proteins will non heme is found within plants with a total of 95% of iron found within the human body is in the form of heme iron [1].

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