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

• 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.

• 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.

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

• 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.

• 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.

• 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.

• 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.

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

• 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.

• 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.

• John KendrewRelated: Perutz’s parallel structure determination extended the protein-structure breakthrough beyond myoglobin.

• Blood agentRelated: Carbon monoxide disrupts oxygen delivery by binding strongly to hemoglobin.

• HematologyRelated: Its concentration and structure help define major anemia and hemoglobin disorders.

• Hans FischerRelated: Its heme group is the biological setting for the blood pigment Fischer studied.

• HematophagyRelated: It supplies much of blood’s protein and iron to blood-feeding animals.

• Human skin colorRelated: Blood beneath the skin adds red and pink tones to its appearance.

• LuminolRelated: Its heme groups catalyze luminol oxidation, helping produce light where blood is present.

• Microcytic anemiaRelated: Reduced hemoglobin defines anemia, while impaired production often underlies microcytosis.

• AnoxemiaRelated: Most blood oxygen is carried bound to hemoglobin rather than dissolved in plasma.

• Group 8 elementRelated: Iron's reversible oxygen binding makes it essential to hemoglobin's function.

• John Scott HaldaneRelated: Haldane investigated how blood chemistry governs oxygen carriage and respiratory responses.

• Wild yakRelated: Blood oxygen transport is central to coping with the thin air of high elevations.

• Circulatory and Respiratory Physiological PhenomenaRelated: Its binding lets blood carry far more oxygen than plasma can dissolve.

• Erythroid cellsRelated: Erythroid cells accumulate this protein as they acquire their oxygen-carrying function.

• Pallor mortisRelated: The loss of blood from superficial vessels removes a major source of skin coloration.

• RiftiaRelated: Riftia’s unusual hemoglobin binds both oxygen and sulfide, delivering them to its symbionts.