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The 71 pages that link to Hemoglobin, each with the reason it gives.

• ProteinBroader topic: Its reversible oxygen binding is a clear example of protein-mediated transport.

• Coordination complexBroader topic: Its iron center binds oxygen reversibly within a protein-bound coordination site.

• IronBroader topic: Its heme groups bind oxygen through iron atoms.

• Transition metalRelated: Its iron center binds oxygen reversibly, linking transition-metal coordination to respiration.

• AnemiaRelated: Low hemoglobin concentration is one defining basis for diagnosing anemia.

• Complete blood countRelated: Hemoglobin concentration is a core measure of red-cell oxygen-carrying capacity.

• Carbon monoxide poisoningBroader topic: Carbon monoxide binds hemoglobin far more strongly than oxygen, disrupting oxygen transport.

• MelaninCompared with: Blood color can affect tissue appearance, but hemoglobin is not a melanin pigment.

• ChelationRelated: The porphyrin ligand chelates iron at the core of each heme group.

• Pulse oximetryRelated: Pulse oximetry infers oxygen binding by analyzing hemoglobin’s wavelength-dependent absorption.

• Iron deficiency anemiaRelated: Iron is part of heme, so shortages directly restrict hemoglobin synthesis.

• Nitric oxideRelated: Hemoglobin rapidly removes NO from blood, limiting its signaling range.

• ChlorophyllCompared with: Its colored heme group is often compared with chlorophyll’s green, magnesium-centered ring, despite different structures and functions.

• LigandBroader topic: The heme iron binds oxygen reversibly, with the protein environment influencing ligand binding.

• Red blood cellRelated: Its reversible oxygen binding makes red blood cells the blood’s main oxygen carriers.

• MyoglobinCompared with: Comparing it with myoglobin reveals the difference between oxygen transport and muscle storage.

• Sickle cell diseaseNarrower topic: Sickle cell disease begins with a change in one of hemoglobin’s globin chains.

• Gas exchangeRelated: Hemoglobin increases blood's oxygen-carrying capacity after oxygen enters the lungs.

• HemeRelated: Its four heme groups bind oxygen for transport through the blood.

• Respiratory systemRelated: It carries most oxygen from the lungs to body tissues.

• ErythropoietinRelated: More erythropoietin-driven red cells generally increase the blood's oxygen-carrying capacity.

• MethemoglobinemiaNarrower topic: Oxidation alters hemoglobin’s iron and changes its oxygen-binding behavior.

• Pulmonary circulationRelated: Its oxygen loading in the lungs gives pulmonary venous blood its high oxygen content.

• BloodRelated: Its oxygen binding enables red blood cells to transport oxygen efficiently.

• Gastrointestinal bleedingRelated: Its concentration helps clinicians track the consequences of bleeding.

• HemolysisRelated: Its release is the most visible biochemical consequence of red-cell rupture.

• Hemolytic anemiaRelated: Its release and breakdown account for several laboratory and clinical signs of hemolysis.

• Iron deficiencyRelated: Iron shortage limits heme production and can reduce hemoglobin concentration.

• BilirubinRelated: Its heme groups supply a major share of the body’s bilirubin.

• Diving physiologyRelated: Large blood oxygen stores depend partly on hemoglobin concentration and blood volume.

• Allosteric regulationBroader topic: Oxygen binding is cooperative, and protons, carbon dioxide, and 2,3-bisphosphoglycerate regulate its affinity.

• BicarbonateRelated: Hemoglobin buffers protons produced alongside bicarbonate and supports carbon dioxide carriage.

• Altitude trainingRelated: Changes in red-cell mass can alter the blood’s capacity to carry oxygen.

• Blood donationRelated: Hemoglobin levels help assess donor eligibility and red-cell function.

• PorphyrinRelated: Its heme porphyrins make oxygen transport possible.

• SpleenRelated: Splenic macrophages recover and recycle iron from hemoglobin in removed cells.

• Max PerutzBroader topic: Its atomic structure was the central object of Perutz’s crystallographic research.

• NitriteRelated: Nitrite can oxidize hemoglobin, while related pigment chemistry helps explain cured-meat color.

• Circulatory systemRelated: Its reversible oxygen binding enables blood to load and release oxygen.

• Oxygen–hemoglobin dissociation curveNarrower topic: Its oxygen-binding behavior generates the curve.

• Protein crystallographyBroader topic: Its structure became a landmark target in the development of protein crystallography.

• ReticulocyteRelated: Reticulocytes continue accumulating hemoglobin as they complete maturation.

• Hemoglobin A1cNarrower topic: A1c is a glycated form of this protein.

• Cardiorespiratory fitnessRelated: Its concentration and function affect how much oxygen blood can carry.

• Iron(II)Related: Its heme iron binds oxygen while remaining in the ferrous state.

• Aerobic capacityRelated: Blood oxygen transport depends largely on hemoglobin concentration and saturation.

• CyanosisNarrower topic: Cyanosis reflects the color or quantity of hemoglobin in superficial blood.

• Bohr effectNarrower topic: Its changing oxygen affinity is the basis of the Bohr effect.

• High-altitude adaptationRelated: Changes in hemoglobin’s oxygen affinity can alter oxygen uptake in thin air.

• Near-infrared spectroscopyRelated: Its oxygenated and deoxygenated forms absorb near-infrared light differently.